Receptors for hypersensitive response elicitors and uses thereof

ABSTRACT

The present invention is directed to an isolated protein which serves as a receptor in plants for a plant pathogen hypersensitive response elicitor. Also disclosed are nucleic acid molecules encoding such receptors as well as expression vectors, host cells, transgenic plants, and transgenic plant seeds containing such nucleic acid molecules. Both the protein and nucleic acid can be used to identify agents targeting plant cells to enhance a plant&#39;s receptivity to treatment with a hypersensitive response elicitor and to directly impart plant growth enhancement as well as resistance against disease, insects, and stress.

[0001] The present application is continuation-in-part of U.S. patent application Ser. No. 09/810,997, filed Mar. 16, 2001, and claims benefit of U.S. Provisional Patent Application Serial No. 60/335,776, filed Oct. 31, 2001.

FIELD OF THE INVENTION

[0002] The present invention relates to receptors for hypersensitive response elicitors and uses thereof.

BACKGROUND OF THE INVENTION

[0003] Plants have evolved a complex array of biochemical pathways that enable them to recognize and respond to environmental signals, including pathogen infection. There are two major types of interactions between a pathogen and plant—compatible and incompatible. When a pathogen and a plant are compatible, disease generally occurs. If a pathogen and a plant are incompatible, the plant is usually resistant to that particular pathogen. In an incompatible interaction, a plant will restrict pathogen proliferation by causing localized necrosis, or death of tissues, to a small zone surrounding the site of infection. This reaction by the plant is defined as the hypersensitive response (“HR”) (Kiraly, Z. “Defenses Triggered by the Invader: Hypersensitivity,” Plant Disease: An Advanced Treatise 5:201-224 J. G. Horsfall and E. B. Cowling, eds. Academic Press, New York (1980); (Klement “Hypersensitivity,” Phytopathogenic Prokaryotes 2:149-177, M. S. Mount and G. H. Lacy, eds. Academic Press, New York (1982)). The localized cell death not only contains the infecting pathogen from spreading further but also leads to a systemic resistance preventing subsequent infections by other pathogens. Therefore, HR is a common form of plant resistance to diseases caused by bacteria, fungi, nematodes, and viruses.

[0004] A set of genes designated as hrp (Hypersensitive Response and Pathogenicity) is responsible for the elicitation of the HR by pathogenic bacteria, including Erwinia spp, Pseudomonas spp, Xanthomonas spp, and Ralstonia solanacearum (Willis et al. “hrp Genes of Phytopathogenic Bacteria,” Mol. Plant-Microbe Interact. 4:132-138 (1991), Bonas, U. “hrp Genes of Phytopathogenic Bacteria,” pages 79-98 in: Current Topics in Microbiology and Immunology, Vol. 192, Bacterial Pathogenesis of Plants and Animals: Molecular and Cellular Mechanisms. J. L. Dangl, ed. Springer-Verlag, Berlin (1994); Alfano et al., “Bacterial Pathogens in Plants: Life Up Against the Wall,” Plant Cell 8:1683-98 (1996). Typically, there are multiple hrp genes clustered in a 30-40 kb segments of DNA. Mutation in any one of the hrp genes will result in the loss of bacterial pathogenicity in host plants and the HR in non-host plants. On the basis of genetic and biochemical characterization, the function of the hrp genes can be classified into three groups: 1) structural genes encoding extracellularly located HR elicitors, for example harpin of Erwinia amylovora (Wei et al. “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85 (1992)); 2) secretion genes encoding a secretory apparatus for exporting HR elicitors and other proteins from the bacterial cytoplasm to the cell surface or extracellular space (Van Gijsegem et al., “Evolutionary Conservation of Pathogenicity Determinants Among Plant and Animal Pathogenic Bacteria,” Trends Microbiol. 1:175-180 (1993); He et al, “Pseudomonas syringae pv. Syringae harpin_(pss): A Protein that is Secreted Via the Hrp Pathway and Elicits the Hypersensitive Response in Plants,” Cell 73:1255 (1993); Wei et al., “HrpI of Erwinia amylovora Functions in Secretion of Harpin and is a Member of a New Protein Family,” J. Bacteriol. 175:7985-67 (1993), Arlat et al. “PopA1, a Protein which Induces a Hypersensitive-Like Response on Specific Petunia Genotypes, is Secreted via the Hrp Pathway of Pseudomonas solanacearum,” EMBO J. 13:543-53 (1994), Galan et al., “Cross-talk between Bacterial Pathogens and their Host Cells,” Ann. Rev. Cell Dev. Biol. 12:221-55 (1996); Bogdanove et al., “Erwinia amylovora Secretes Harpin via a Type III Pathway and Contains a Homolog of yopN of Yersinia,” J. Bacteriol. 178:1720-30 (1996); Bogdanove et al., “Homology and Functional Similarity of a hrp-linked Pathogenicity Operon, dspEF, of Erwinia amylovora and the avrE locus of Pseudomonas syringae pathovar tomato,” Proc Natl Acad Sci USA 95:1325-30 (1998)); and 3) regulatory genes that control the expression of hrp genes (Wei, Z. M., “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85 (1992); Wei et al., “hrpL Activates Erwinia amylovora hrp Genes in Response to Environmental Stimuli,” J. Bacteriol. 174:1875-82 (1995); Xiao et al., “A Single Promoter Sequence Recognized by a Newly Identified Alternate Sigma Factor Directs Expression of Pathogenicity and Host Range Determinants in Pseudomonas syringae,” J. Bacteriol 176:3089-91 (1994); Kim et al., “The hrpA and hrpC Operons of Erwinia amylovora Encode Components of a Type III Pathway that Secretes Harpin,” J. Bacteriol 179:1690-97 (1997); Kim et al., “HrpW of Erwinia amylovora, a New Harpin that Contains a Domain Homologous to Pectate Lyases of a Distinct Class,” J. Bacteriol. 180:5203-10 (1998); Wengelnik et al., “HrpG, A Key hrp Regulatory Protein of Xanthomonas campestris pv. Vesicatoria is Homologous to Two Component Response Regulators,” Mol. Plant-Microbe Interact. 9:704-12 (1996)). Because of their role in interactions between plants and microbes, hrp genes have been a focus for bacterial pathogenicity and plant defense studies.

[0005] In addition to the local defense response, HR also activates the defense system in uninfected parts of the same plant. This results in a general systemic resistance to a secondary infection termed Systemic Acquired Resistance (“SAR”) (Ross, R. F. “Systemic Acquired Resistance Induced by Localized Virus Infections in Plants,” Virology 14:340-58 (1961); Malamy et al., “Salicylic Acid and Plant Disease Resistance,” Plant J. 2:643-654 (1990)). SAR confers long-lasting systemic disease resistance against a broad spectrum of pathogens and is associated with the expression of a certain set of genes (Ward et al. “Coordinate Gene Activity in Response to Agents that Induce Systemic Acquired Resistance,” Plant Cell 3:1085-94 (1991)). SAR is an important component of the disease resistance of plants and has long been of interest, because the potential of inducing the plant to protect itself could significantly reduce or eliminate the need for chemical pesticides. SAR can be induced by biotic (microbes) or abiotic (chemical) agents (Gorlach et al. “Benzothiadiazole, a Novel Class of Inducers of Systemic Acquired Resistance, Activates Gene Expression and Disease Resistance in Wheat,” Plant Cell 8:629-43 (1996)). Historically, weak virulent pathogens were used as a biotic inducing agent for SAR. Non-virulent plant growth promotion bacteria (“PGPR”) were also reported to be able to induce resistance of some plants against various diseases. Biotic agent-induced SAR has been the subject of much research, especially in the late 70s and early 80s. Only very limited success was achieved, however, due to: 1) inconsistency of the performance of living organisms in different environmental conditions; 2) considerable concerns regarding the unpredictable consequences of the intentional introduction of weakly virulent pathogens into the environment; and 3) the technical complication of applying a living microorganism into a variety of environmental conditions. To overcome the limitations of using living organisms to induce SAR, scientists have long been looking for an HR elicitor derived from a pathogen for SAR induction. With the advancement of molecular biology, the first proteinaceous HR elicitor with broad host spectrum was isolated in 1992 from Erwinia amylovora, a pathogenic bacterium causing fire blight in apple and pear. The HR elicitor was named “harpin”. It consists of 403 amino acids with a molecular weight about 40 kDa. The harpin protein is heat-stable and glycine-rich with no cysteine. The gene encoding the harpin protein is contained in a 1.3 kb DNA fragment located in the middle of the hrp gene cluster. Harpin is secreted into the extracellular space and is very sensitive to proteinase digestion. Since the first harpin was isolated from Erwinia amylovora, several harpin or harpin-like proteins have been isolated from other major groups of plant pathogenic bacteria. In addition to the harpin of Erwinia amylovora, the following harpin or harpin-like proteins have been isolated and characterized: HrpN of Erwinia chrysanthemi, Erwinia carotovora (Wei et al. “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science, 257:85 (1992)), and Erwinia stewartii; HrpZ of Pseudomonas syringae (He et al, “Pseudomonas syringae pv. Syringae harpin _(pss): A Protein that is Secreted Via the Hrp Pathway and Elicits the Hypersensitive Response in Plants,” Cell 73:1255 (1993)), PopA of Ralstonia solanacearum, (Arlat et al. “PopA1, a Protein which Induces a Hypersensitive-Like Response on Specific Petunia Genotypes, is Secreted via the Hrp Pathway of Pseudomonas solanacearum,” EMBO J. 13:543-53 (1994)); HrpW of Erwinia amylovora (Kim et al., “HrpW of Erwinia amylovora, a New Harpin that Contains a Domain Homologous to Pectate Lyases of a Distinct Class,” J. Bacteriol. 180:5203-10 (1998)), and Pseudomonas syringae. All of the currently described harpin or harpin-like proteins share common characteristics. They are heat-stable and glycine-rich proteins with no cysteine amino acid residue, are very sensitive to digestion by proteinases, and elicit the HR and induce resistance in many plants against many diseases. Based on their shared biochemical and biophysical characteristics as well as biological functions, these HR elicitors from different pathogenic bacteria belong to a new protein family—i.e. the harpin protein family. The described characteristics, especially their ability to induce HR in a broad range of plants, distinguish the harpin protein family from other host specific proteinaceous HR elicitors, for example elicitins from Phytophthora spp (Bonnet et al., “Acquired Resistance Triggered by Elicitors in Tobacco and Other Plants,” Eur. J. Plant Path. 102:181-92 (1996); Keller, et al. “Physiological and Molecular Characteristics of Elicitin-Induced Systemic Acquired Resistance in Tobacco,” Plant Physiol 110:365-76 (1996)) or avirulence proteins (such as Avr9) from Cladosporium fulvum, which are only able to elicit the HR in a specific variety or species of a plant.

[0006] In nature, when certain bacterial infections occur, harpin protein is expressed and then secreted by the bacteria, signaling the plant to mount a defense against the infection. Harpin serves as a signal to activate plant defense and other physiological systems, which include SAR, growth enhancement, and resistance to certain insect damage.

[0007] The current understanding of critical plant molecules that may have a significant role in interacting with elicitors and then triggering a sequential signal transduction cascade is described as follows.

[0008] Interaction of Plant Resistance Genes (R) and Pathogen Avirulence Genes (avr)

[0009] The concept of gene-for-gene interaction is that “for each gene determining resistance (R gene) in the host, there is a corresponding gene determining avirulence in the pathogen (avr gene)”. In this model, pathogen avirulence genes generate a specific ligand molecule, called an elicitor. Only plants carrying the matching resistance gene respond to this elicitor and invoke the HR. In the past few years, several disease-resistance, R genes, have been cloned and sequenced. It was expected that R genes might encode components involved in signal recognition or signal transduction pathways that ultimately lead to defense responses. The cloned R genes could be grouped into four classes: (1) cytoplasmic protein kinase; (2) protein kinases with an extracellular domain; (3) cytoplasmic proteins with a region of leucine-rich repeats and a nucleotide-binding site; and (4) proteins with a region of leucine-rich repeats that appear to encode extracellular proteins. (Review in Bent, A. F. “Plant Disease Resistance Genes: Function Meets Structure,” Plant Cell 8: 1757-71 (1996); Baker B., et al., “Signaling in Plant-Microbe Interactions,” Science 276:726-33 (1997)). The first R gene cloned, Pto, encodes a serine/threonine protein kinase. The protein product of Pto directly interacts with the cognate avirulence gene protein, AvrPro, which has been demonstrated in a yeast two-hybrid system. It was shown that only co-existence of both AvrPro and Pto proteins could elicit HR in plants (Tang et al., “Initiation of Plant Disease Resistance by Physical Interaction of AvrPto and Pto kinase,” Science 274:2060-63 (1996); Scofield et al., “Molecular Basis of Gene-for-Gene Specificity in Bacterial Speck Disease of Tomato,” Science 274:2063-65 (1996); Zhou et al., “The Pto Kinase Conferring Resistance to Tomato Bacterial Speck Disease Interacts with Proteins that Bind a cis-element of Pathogenesis-related Genes,” EMBO J. 16:3207-18 (1997)). The results from cloned R genes support the view that plant-pathogen interactions involve protein-protein interactions. Syringolide, a water-soluble, low-molecular-weight elicitor, triggers a defense response in soybean cultivars carrying the Rpg4 disease-resistance gene. A 34-KDa protein has been isolated from soybean and is considered to be the physiological active syringolide receptor (Ji et al., “Characterization of a 34-kDa Soybean Binding Protein for the Syringolide Elicitors,” Proc. Natl. Acad. Sci. USA 95:3306-11 (1998)).

[0010] Putative Binding Factor of Elicitin

[0011] Elicitins are a family of small proteins secreted by Phytophthora species that have a high degree of homology. Pure elicitins alone can cause a hypersensitive response, a local cell death, and trigger systemic acquired resistance in tobacco and other plants (Bonnet et al., “Acquired Resistance Triggered by Elicitors in Tobacco and Other Plants,” Eur. J. Plant Path. 102:181-92 (1996); Keller, et al. “Physiological and Molecular Characteristics of Elicitin-Induced Systemic Acquired Resistance in Tobacco,” Plant Physiol 110:365-76 (1996)). However, the spectrum of HR elicitation and induced systemic resistance in plants is much narrower than that achieved by harpin family elicitors. Like harpin, elicitins induce a series of metabolic events in tobacco cells, including the accumulation of phytoalexins, ethylene production, transmembrane electrolyte leakage, H₂O₂ accumulation, and expression of plant defense related genes (Yu L, et al., “Elicitins from Phytophthora and Basic Resistance in Tobacco,” Proc. Natl. Acad. Sci. (1995); Keller et al., “Pathogen-Induced Elicitin Production in Transgenic Tobacco Generates a Hypersensitive Response and Nonspecific Disease Resistance,” The Plant Cell 11:223-35 (1999)). A putative receptor-like binding factor has been identified in tobacco plasma membrane, which has a specific high-affinity to the crytogein, one member of the elicitin family (Wendehenne, et al., “Evidence for Specific, High-Affinity Binding Sites for a Proteinaceous Elicitor in Tobacco Plasma Membrane,” FEBS Letters 374:203-207 (1995)). Recently, it was found that 2 basic elicitins (i.e. cryptogein and cinnamomin) and two acidic elicitins (i.e. capsicein and parasiticein) were able to interact with the same binding sites on tobacco plasma membranes (Bourque et al., “Comparison of Binding Properties and Early Biological Effects of Elicitins in Tobacco Cells,” Plant Physiol. 118:1317-26 (1998)). However, the gene of the receptor-like factor has not been isolated.

[0012] Putative Binding Factor of Glycoprotein Elicitors

[0013] A 42 kDa glycoprotein elicitor has been isolated from Phytophthora megasperma (Parker et al., “An Extracellular Glycoprotein from Phytophthora megasperma f. sp. glycinea Elicits Phytoalexin Synthesis in Cultured Parsley Cells and Protoplasts,” Mol. Plant Microbe Interact. 4:19-27 (1991)). An oligopeptide of 13 amino acids within the glycoprotein (“Pep-13”) was able to induce a response in plants like that achieved by the full glycoprotein. A high affinity-binding pattern has been observed in parsley microsomal membranes with an isotope labeled oligopeptide. There are estimated to be about 1600 to 2900 binding sites per cell with evidence indicating that a low abundance protein receptor of the Pep-13 is localized in the plasma membrane (Nurnberger et al., “High Affinity Binding of a Fungal Oligopeptide Elicitor to Parsley Plasma Membranes Triggers Multiple Defense Responses,” Cell 78:449-60 (1994)).

[0014] Harpin Protein Binding Factors

[0015] Harpin proteins, which elicit HR in a variety of different nonhost plants, have been isolated from plant pathogens (Wei et al. “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85 (1992)). A family of harpin proteins has been identified from plant bacterial pathogens. All of them have similar biological activities. It is well documented that harpin protein can induce plants to produce active oxygen, change ion flux, lead to local cell death, and induce systemic acquired resistance (“SAR”) (Wei et al. “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85 (1992); He et al., “Pseudomonas syringae pv. syringae Harpin_(Pss): A Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants,” Cell 73:1255-66 (1993); Baker, C. J., et al., “Harpin, an Elicitor of the Hypersensitive Response in Tobacco Caused by Erwinia amylovora, Elicits Active Oxygen Production in Suspension Cells,” Plant Physiol. 102:1341-44 (1993)). No harpin protein binding factor has been isolated so far. It was reported that an amphipathic protein, named HRAP, isolated from sweet pepper could dissociate harpin_(pss) in multimeric form (hrpZ from Pseduomonas syringae). The biological activity of the HAAP is believed to be its ability to intensify harpin_(pss)-mediated hypersensitive response. HRAP protein does not bind to harpin_(pss) directly (Chen et al., “An Amphipathic Protein from Sweet Pepper can Dissociate Harpin_(pss) Multimeric Forms and Intensify the Harpin_(pss)-Mediated Hypersensitive Response,” Physiological & Molecular Pathology 52:139-49 (1998)). Using a fluorochrome tagged antibody to harpin to examine the interaction of harpin_(pss) and tobacco suspension cells, it was found that harpin_(pss) interacted with the cultured cells, but not with protoplasts with the cell walls being digested and removed. It was interpreted that harpin_(pss) was localized in the outer portion of the plant cell, probably on the cell well. However, it was not ruled out that the binding factor was located on the plasma membrane.

[0016] The present invention seeks to identify receptors for hypersensitive response elicitor proteins or polypeptides and uses of such receptors.

SUMMARY OF THE INVENTION

[0017] The present invention is directed to an isolated protein which serves as a receptor in plants for a plant pathogen hypersensitive response elicitor. Also disclosed are nucleic acid molecules encoding such receptors as well as expression vectors, host cells, transgenic plants, and transgenic plant seeds containing such nucleic acid molecules.

[0018] The protein of the present invention can be used with a method of identifying agents targeting plant cells by forming a reaction mixture including the protein and a candidate agent, evaluating the reaction mixture for binding between the protein and the candidate agent, and identifying candidate compounds which bind to the protein in the reaction mixture as plant cell targeting agents.

[0019] The nucleic acid molecule of the present invention can be used in a method of identifying agents targeting plant cells by forming a reaction mixture including a cell transformed with the nucleic acid molecule of the present invention and a candidate agent, evaluating the reaction mixture for binding between protein produced by the host cell and candidate agent, and identifying candidate compounds which bind to the protein or the host cell in the reaction mixture as plant cell targeting agents.

[0020] Another aspect of the present invention relates to a method of enhancing a plant's receptivity to treatment with hypersensitive response elicitors by providing a transgenic plant or transgenic plant seed transformed with the nucleic acid molecule of the present invention.

[0021] The present invention is also directed to a method of imparting disease resistance, enhancing growth, controlling insects, and/or imparting stress resistance to plants by providing a transgenic plant or transgenic plant seed transformed with a DNA construct effective to silence expression of a nucleic acid molecule encoding a receptor in accordance with the present invention.

[0022] The discovery of the present invention has great significance. This putative receptor protein can be used as a novel way to screen for new inducers of plant resistance against insect, disease, and stress, and of growth enhancement. This protein is the first step toward the understanding of the harpin induced signal transduction pathway in plants. Further studies of this pathway will provide more possible targets for new plant vaccine and growth enhancement products development. In addition, this protein can serve as an anchor providing a new way to target anything to the plant cells.

BRIEF DESCRIPTION OF THE DRAWINGS

[0023]FIG. 1 shows a yeast two-hybrid screening with the Erwinia amylovora hypersensitive response elicitor (i.e. harpin) and a schematic representation of the interaction between harpin and a cDNA encoded polypeptide. Harpin is fused to a LexA protein which contains a DNA binding domain (“BD”). The cDNA encoded polypeptide is fused to the GAL4 transcription activation domain (“AD”). This interaction targets the activation domain to two different LexA-dependent promoters with consequent activation of the transcription of the HIS3 and lacZ reporter genes.

[0024] FIGS. 2A-B show that the Erwinia amylovora hypersensitive response elicitor (i.e. harpin) is a good yeast two-hybrid bait. Reporter genes were not expressed in yeast strain L40 containing plasmids expressing the LexA—harpin fusion in combination with plasmids expressing the GAL4 activation domain alone, or fused to unrelated protein. Therefore, harpin is not autoactive in this yeast two-hybrid system. In addition, reporter genes were not expressed in yeast strain L40 containing plasmids expressing the GAL4 activation domain-harpin fusion in combination with plasmids expressing LexA alone, or fused to unrelated protein. FIG. 2A shows a galactosidase assay where blue color indicates the expression of lacZ reporter gene. FIG. 2B shows a synthetic minimal (“SD”) media plate which lacks leucine, tryptophan, and histidine. Growth on such a plate indicates the expression of the HIS3 reporter gene.

[0025] FIGS. 3A-B show the interaction between AtHrBP1p (hypersensitive response elicitor binding protein 1) and a hypersensitive response elicitor (i.e. harpin) is specific. Reporter genes were expressed in yeast strain L40 containing plasmids expressing the GAL4 activation domain-AtHrBP1 fusion in combination with plasmids expressing LexA fused to hypersensitive response elicitor (i.e. harpin), but were not expressed in combination with LexA alone, or LexA fused to unrelated proteins. FIG. 3A is a β-galactosidase assay where the blue color indicates the expression of lacZ reporter gene. FIG. 3B is an SD media plate which lacks leucine, tryptophan, and histidine. Growth on such a plate indicates the expression of the HIS3 reporter gene.

[0026] FIGS. 4A-B show the interaction of HrBP1p and a hypersensitive response elicitor (i.e. harpin) in another orientation. Reporter genes were expressed in yeast strain L40 containing plasmids expressing the LexA-AtHrBP1p fusion in combination with plasmids expressing GAL4 activation domain fused to harpin, but were not expressed in combination with GAL4 activation domain alone, or GAL4 activation domain fused to unrelated proteins. Therefore, interaction between harpin and HrBP1p is specific. FIG. 4A shows a β-galactosidase assay where blue color indicates the expression of lacZ reporter gene. FIG. 4B shows an SD media plate which lacks leucine, tryptophan, and histidine. Growth on such a plate indicates the expression of the HIS3 reporter gene.

[0027]FIG. 5 shows the gene structure of,AtHrBP1 and a schematic representation of the exons and introns of the AtHrBP1 gene. When comparing the AtHrBP1 cDNA sequence with the Arabidopsis thaliana genomic DNA sequence published in a public database, four exons and three introns were discovered.

[0028]FIG. 6 shows a Northern blot using RNA probe complementary to bases 651-855 of AtHrBP1 coding region (SEQ. ID. No. 29).

[0029] FIGS. 7A-B show that the interaction between rice HrBP1p (R6p) and harpin is specific. Reporter genes were expressed in yeast strain L40 containing plasmids expressing the GAL4 activation domain-rice HrBP1p fusion in combination with plasmids expressing LexA fused to harpin or harpin 137-180 amino acids, but were not expressed in combination with LexA alone, LexA fused to unrelated proteins, or fused to harpin 210-403 amino acids. FIG. 7A shows a β-galactosidase assay where blue color indicates the expression of the lacZ reporter gene. FIG. 7B shows an SD media plate, which lacks leucine, tryptophan, and histidine. Growth on such a plate indicates the expression of the HIS3 reporter gene.

[0030]FIG. 8 shows an alignment of HrBP1p amino acid sequences for the receptors from cotton, soybean, barley, tomato, rice, potato, wheat, maize, grapefruit, apple, tobacco, grape, and Arabidopsis thaliana.

[0031]FIG. 9 shows a chart of the AtHrBP1p full-length and truncated polypeptides that were screened for their ability to interact with the harpin protein. The different HrBP1p fragments were utilized in the yeast-two hybrid system along with the harpin protein.

[0032]FIG. 10 shows the purified proteins used for in vitro binding studies. 1.2-1.5 μg of protein/lane was electrophoresed on a denaturing 10% polyacrylamide gel and stained with coomassie blue. Lane 1, standards; lane 2, HrpN; lane 3, HrBP1p; lane 4, TL-HrBP1p. The molecular masses of the standards are indicated on the left side of Lane 1.

[0033] FIGS. 11A-B show that AtHrBP1p interacts specifically with HrpN during affinity chromatography. Partially purified HrBP1p was mixed with HrpN-conjugated (HrpN) or mock-conjugated (C) agarose beads in binding buffer (20 mM Tris HCl, 50 mM NaCl, 0.2 mM EDTA, 1 mM DTT) and the beads were washed ten times with binding buffer (4 to 10 bed volumes each). Successive step elutions were done in binding buffer containing 200, 500, 750, 1000, and 1500 mM NaCl (2 bed volumes each). Selected fractions were run on denaturing 10% polyacryamide gels and the proteins were stained with silver. In FIG. 11A, the buffers contained no detergent. In FIG. 11B, the binding, wash, and elution buffers all contained 0.2% CHAPS. Horizontal arrows show the position of AtHrBP1p. The diagonal arrow points to HrpN. The molecular masses of the standards are indicated on the left side of each gel.

[0034]FIG. 12 shows the constructs used to “knockout” AtHrBP1 gene in Arabidopsis.

[0035] FIGS. 13A-C show a Pseudomonas syringae p.v. tomato DC3000 assay on wild type and AtHrBP1 “knockout” transgenic Arabidopsis plants. FIG. 13A is a picture taken 7 days after P. syringae inoculation. In FIG. 13B, leaf disks were harvested. Bacteria were extracted from leaf disks and plated onto King's B agar plate containing 100 μg rifampicin/ml. FIG. 13C shows the bacteria count from plates in FIG. 13B. The prefix “as” signifies an anti-sense line and “d” refers to a double-stranded RNA line.

[0036] FIGS. 14A-B show results from a study evaluating the differences in growth between wild type Arabidopsis thaliana and AtHrBP1 transgenic plant lines. There were 10 plant per line, except line 14-7, which had 9 plants. In FIG. 14A, the percentage of plants with 4 true leaves>1 mm in length was determined at sequential days after sowing. FIG. 14B shows the average diameter of maximum rosette radius of the plants when they entered the four-leaf stage. The standard deviation for each test group is indicated in the figure.

[0037]FIG. 15 shows wild type Arabidopsis thaliana and AtHrBP1 transgenic plant lines 32 days after sowing. Stems of the AtHrBP1 transgenic plants were more elongated than those of the wild type plants.

[0038]FIG. 16 shows the construct used to overexpress AtHrBP1 in tobacco.

[0039] FIGS. 17A-B show the height of wild type and AtHrBP1 overexpressing tobacco plants 52 days after they were transferred to soil. FIG. 17A is a picture taken 52 days after plants were transferred to soil. FIG. 17B shows average height of 8 plants per line.

[0040] FIGS. 18A-B show the results of a TMV assay on wild type and AtHrBP1 overexpressing tobacco plants. FIG. 18A is a picture taken 3 days after TMV inoculation. FIG. 1 8B shows the average virus lesion diameter from 5 plants per line 3 days after TMV inoculation.

[0041]FIG. 19 shows the 52-day-old wild type and two independent AtHrBP1p over-expressing Xanthi NN tobacco plants inoculated with Pseudomonas solanacearum, by root cutting.

DETAILED DESCRIPTION OF THE INVENTION

[0042] The present invention is directed to isolated receptors for hypersensitive response elicitor proteins or polypeptides. Also disclosed are DNA molecules encoding such receptors as well as expression systems, host cells, and plants containing such molecules. Uses of the receptors themselves and the DNA molecules encoding them are disclosed. The receptor for a hypersensitive response elicitor from a plant pathogen can be from a monocot or a dicot.

[0043] One example of such a receptor is that found in Arabidopsis thaliana which has the amino acid sequence of SEQ. ID. No. 1 as follows: Met Ala Thr Ser Ser Thr Phe Ser Ser Leu Leu Pro   1               5                  10 Ser Pro Pro Ala Leu Leu Ser Asp His Arg Ser Pro          15                  20 Pro Pro Ser Ile Arg Tyr Ser Phe Ser Pro Leu Thr  25                  30                   35 Thr Pro Lys Ser Ser Arg Leu Gly Phe Thr Val Pro              40                  45 Glu Lys Arg Asn Leu Ala Ala Asn Ser Ser Leu Val      50                  55                  60 Glu Val Ser Ile Gly Gly Glu Ser Asp Pro Pro Pro                  65                  70 Ser Ser Ser Gly Ser Gly Gly Asp Asp Lys Gln Ile          75                  80 Ala Leu Leu Lys Leu Lys Leu Leu Ser Val Val Ser  85                  90                  95 Gly Leu Asn Arg Gly Leu Val Ala Ser Val Asp Asp             100                 105 Leu Glu Arg Ala Glu Val Ala Ala Lys Glu Leu Glu     110                 115                 120 Thr Ala Gly Gly Pro Val Asp Leu Thr Asp Asp Leu                 125                 130 Asp Lys Leu Gln Gly Lys Trp Arg Leu Leu Tyr Ser         135                 140 Ser Ala Phe Ser Ser Arg Ser Leu Gly Gly Ser Arg 145                 150                 155 Pro Gly Leu Pro Thr Gly Arg Leu Ile Pro Val Thr             160                 165 Leu Gly Gln Val Phe Gln Arg Ile Asp Val Phe Ser     170                 175                 180 Lys Asp Phe Asp Asn Ile Ala Glu Val Glu Leu Gly                 185                 190 Ala Pro Trp Pro Phe Pro Pro Leu Glu Ala Thr Ala         195                 200 Thr Leu Ala His Lys Phe Glu Leu Leu Gly Thr Cys 205                 210                 215 Lys Ile Lys Ile Thr Phe Glu Lys Thr Thr Val Lys             220                 225 Thr Ser Gly Asn Leu Ser Gln Ile Pro Pro Phe Asp     230                 235                 240 Ile Pro Arg Leu Pro Asp Ser Phe Arg Pro Ser Ser                 245                 250 Asn Pro Gly Thr Gly Asp Phe Glu Val Thr Tyr Val         255                 260 Asp Asp Thr Met Arg Ile Thr Arg Gly Asp Arg Gly 265                 270                 275 Glu Leu Arg Val Phe Val Ile Ala             280

[0044] This protein, known as AtHrBP1p, is encoded by a cDNA molecule having SEQ. ID. No. 2 as follows: tttttccttc tcaacaatgg cgacttcttc tactttctcg tcactactac cttcaccacc 60 agctcttctt tccgaccacc gttctcctcc accatccatc agatactcct tttctccctt 120 aactactcca aaatcgtctc gtttgggttt cactgtaccg gagaagagga acctcgctgc 180 taattcgtct ctcgttgaag tatccattgg cggagaaagt gacccaccac catcatcatc 240 tggatcagga ggagacgaca agcaaattgc attactcaaa ctcaaattac ttagtgtagt 300 ttcgggatta aacagaggac ttgtggcgag tgttgatgat ttagaaagag ctgaagtggc 360 tgctaaagaa cttgaaactg ctgggggacc ggttgattta accgatgatc ttgataagct 420 tcaagggaaa tggaggctgt tgtatagtag tgcgttctct tctcggtctt taggtggtag 480 ccgtcctggt ctacctactg gacgtttgat ccctgttact cttggccagg tgtttcaacg 540 gattgatgtg tttagcaaag attttgataa catagcagag gtggaattag gagccccttg 600 gccatttccg caattagaag ccactgcgac attggcacac aagtttgaac tcttaggcaa 660 ttgcaagatc aagataacat ttgagaaaac aactgtgaag acatcgggaa acttgtcgca 720 gattcctccg tttgatatcc cgaggcttcc cgacagtttc agaccatcgt caaaccctgg 780 aactggggat ttcgaagtta cctatgttga tgataccatg cgcataactc gcggggacag 840 aggtgaactt agggtattcg tcattgctta attctcaaag ctttgacatg taaagataaa 900 taaatacttt ctgcttgatg cagtctcatg agttttgtac aaatcatgtg aacatataaa 960 tgcgctttat aagtaaatga gtgtcttgtt caatgaatca 1000

[0045] The genomic DNA molecule containing the receptor encoding cDNA molecule of SEQ. ID. No. 2 has SEQ. ID. No. 3 as follows: aattagaaaa attaacaacc aacatctagt tagaatattt aatttgcacc aatgtcttcg 60 agtatagtga aaaaaataga agatcgaata tcgaatagta cgtatagaat catctagatc 120 cattcgaact aacgtctact tttcttttcc agcattaaca tgtagcttgt cattagcatt 180 tacatgttgc aaataacaca aattgggaaa ttgaaagact aaaaaacctt gtacagcaga 240 tggtttaaca cgtggattca tggacacaaa cagaaaacgg cagaactaag cacaaaaacg 300 tcaactaagc atatcaaagc ttttaatgca agcctaatat aaacacaagt ggttatccat 360 aatctgttct taatctcttg cagtagttat cttttcatta ttcgcaattc gcaattctat 420 attcttatat ttcaacttgt tcttcttcca aattgtaatt atatctacat cgtcttagct 480 tgaccattat agctccagta ccaagttctc ttcttaactt taatatcagc tactattctc 540 atactgtaaa tatcttttgt tcaccaaaca tatatttcga accaaactgc taaaagctta 600 tcataaattg cagttctagc cacacaattt tgcagttcca accattaaat gccacaaaat 660 ttggacgatt tcttaagaca agaagaacat agcaaccaaa ccttattgat taaatatgaa 720 atgtctccat aaaactggga gatttcccca aataaagaga acacggcaaa tgttcacgta 780 atctccaaga tgaatgttta attttttctt tcagaaaaaa acaaaaaaac ttaactcaat 840 atagacaact agaatggata ccaactaagc aaaagaaatt caaaagacaa atatatattg 900 gatatgaagt tacattattt tcaaacttta tatactacta aaagcctaaa aatttgttct 960 aaaatgatat ccaaataaat ggaaggcatg aatgtcatat gactaaaaga gaaaaacaca 1020 cctgtatata agtattggat catgctgcct ccgagtgaca aaacatacga tgtgggtctt 1080 tattgggcca tacttaaatg gaaaaaggag aaaaaaaatt gggcaatgtc tatggtcgaa 1140 atttatatgt tttacatcaa taaaatcaat atttaatttt atatatgtgg gtcttaatct 1200 agtattatct acatagatta aaatcaaagt actgcatatg gtccataata atacaaccaa 1260 agcaaattaa aattttgtgg cacaaaacga catcatttta ctcagaaagt aatatgcaat 1320 ttcgtttacg cacacacgta tacgcgctaa taacccgtgg tgcttctcaa atcacataat 1380 aattaaagtc ttcttcttct tcttcttctc tacaaattat ctcactctct tcgttttttt 1440 ttccttctca acaatggcga cttcttctac tttctcgtca ctactacctt caccaccagc 1500 tcttctttcc gaccaccgtt ctcctccacc atccatcaga tactcctttt ctcccttaac 1560 tactccaaaa tcgtctcgtt tgggtttcac tgtaccggag aagagaaacc tcgctgctaa 1620 ttcgtctctc gttgaagtat ccattggcgg agaaagtgac ccaccaccat catcatctgg 1680 atcaggagga gacgacaagc aaattgcatt actcaaactc aaattacttg tgagtctgat 1740 tcaaaccaat cggtgaaatt ataagaaatt ggtttcgttt ctttggaatt agggtttata 1800 ttactgttaa gattcgatta tagagtgaat tttgggaaga tttttcagat ttgatttgtg 1860 atgtgttgtg ttgtgagaaa ttgcagagtg tagtttcggg attaaacaga ggacttgtgg 1920 cgagtgttga tgatttagaa agagctgaag tggctgctaa agaacttgaa actgctgggg 1980 gaccggttga tttaaccgat gatcttgata agcttcaagg gaaatggagg ctgttgtata 2040 gtagtgcgtt ctcttctcgg tctttaggtg gtagccgtcc tggtctacct actggacgtt 2100 tgatccctgt tactcttggc caggtaattc ttgaatcatt gctctgtttt tacccgtcaa 2160 gattcggttt ttcgggtaag ttgttgagga gtttatgtgc atggtctagt ctatcatcaa 2220 tagtcttgct tgagtttgaa tggggctgag ctaagaatct agctttctga ggttacaatt 2280 tggtaatgtc atcttatact cgaaagcaaa cttttttcta tattgtcaag tttatgtgta 2340 cggtctggtc tatcattggt agtctttgtt gagcttgaat ggtgaggagc ttagaatcta 2400 gcaatgtcat ctactcctta atcatttttt tctatattgc caagtttatg tgtacggtct 2460 tagtcaatca tctttattct tggttgagtt tgaatggtga tgagcttaga atctagcttt 2520 ctttggttta aatttggcaa agaaccatac ctgaatcggt agaaagcaaa cttctttaat 2580 attatctctt gtttctgaat cattaaaaca ggtgtttcaa cggattgatg tgtttagcaa 2640 agattttgat aacatagcag aggtggaatt aggagcccct tggccatttc cgccattaga 2700 agccactgcg acattggcac acaagtttga actcttaggt ttgcatttcc ctttctctca 2760 ttaagtttat cgaattgtgt aagagcaaaa taacttatct gtatctttga catttatggg 2820 gaaaacaggc acttgcaaga tcaagataac atttgagaaa acaactgtga agacatcggg 2880 aaacttgtcg cagattcctc cgtttgatat cccgaggctt cccgacagtt tcagaccatc 2940 gtcaaaccct ggaactgggg atttcgaagt tacctatgtt gatgatacca tgcgcataac 3000 tcgcggggac agaggtgaac ttagggtatt cgtcattgct taattctcaa agctttgaca 3060 tgtaaagata aataaatact ttctgcttga tgcagtctca tgagttttgt acaaatcatg 3120 tgaacatata aatgcgcttt ataagtaaat gagtgtcttg ttcaatgaat catatgaaag 3180 aatttgtatg actcagaaaa ttggacaatg atatagacct tccaaatttt gcaccctcta 3240 atgtgagata ttagtgattt tttcttaggt tggtagagag aacggattgg caaaaaaata 3300 tcgaaggtca atgattaaca gcaaaaccat atcttgatga ttcaaaatat agagttaaca 3360 agcaaagatg agacaatctt atacgagaga gctaaaacaa atggattcca aatccagcaa 3420 gtacaaaaat cgcagaaaat aagatgaaac caacttaaaa cagagatgtt ccctttccct 3480 tcttgtcacc accgatctcg aaatgcttgc acctctgaaa taaacaacaa accaacacaa 3540 tgtaagcaaa ttaccaagtt acaaatccgg tataatgaac tgatctatgt tctatgcacc 3600 ttgataggac gctgcgaaaa gtgcttgcag ctttgacact gaagcctcaa aacaatcttc 3660 ttcgtggtct tagcctgtta acaagattca caagatgtat ctcagtccaa aactgagact 3720 attggaatgt ctgtttcctc acagctcact tccaaaattc tactataaat ggttccttaa 3780 aactacctca tttcaactaa ctagacctaa ttcaaactga aaaaacaatc aatgcatgat 3840 aatcaatgtt acctttttgt ggaagacagg cttagtctga ccaccataac cagattgttt 3900 acggtcataa cgacgctttc cttgagcagc aagactgtct ttacccttct tgtattgggt 3960 aaccttgtgc aaagtatgct ttttgcattc cttgttctta cagtaagtgt tctttgtctt 4020 tggaatgttc accttcaaaa ttcataaaat caaaaatgaa tcactcacac acatacaaaa 4080 tcaagagact tttaaggtta atcaaaatac aaacatcatt tagattgaaa acttttatga 4140 tagatctgaa aaacaataca ataaatcaat caaccatgta ttgttgttct tcaaagtcaa 4200 cgaactttac aaattccaaa atcacatcga aagagaagaa acaatttacc attttcgcgt 4260

[0046] Another example of a receptor in accordance with the present invention is that found in rice which has a partial amino acid sequence of SEQ. ID. No. 4 as follows: Val Ala Ala Leu Lys Val Lys Leu Leu Ser Ala Val   1               5                  10 Ser Gly Leu Asn Arg Gly Leu Ala Gly Ser Gln Glu          15                  20 Asp Leu Asp Arg Ala Asp Ala Ala Ala Arg Glu Leu  25                  30                  35 Glu Ala Ala Ala Gly Gly Gly Pro Val Asp Leu Glu              40                  45 Arg Asp Val Asp Lys Leu Gln Gly Arg Trp Arg Leu      50                  55                  60 Val Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly                  65                  70 Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu          75                  80 Pro Ile Thr Leu Gly Gln Val Phe Gln Arg Ile Asp  85                  90                  95 Val Val Ser Lys Asp Phe Asp Asn Ile Val Asp Val             100                 105 Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Val Glu     110                 115                 120 Leu Thr Ala Thr Leu Ala His Lys Phe Glu Ile Ile                 125                 130 Gly Thr Ser Ser Ile Lys Ile Thr Phe Asp Lys Thr         135                 140 Thr Val Lys Thr Lys Gly Asn Leu Ser Gln Leu Pro 145                 150                 155 Pro Leu Glu Val Pro Arg Ile Pro Asp Asn Leu Arg             160                 165 Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe Glu Val     170                 175                 180 Thr Tyr Leu Asp Gly Asp Thr Arg Ile Thr Arg Gly                 185                 190 Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ser         195                 200

[0047] This protein, known as R6p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 5 as follows: cgtggctgcg ctcaaagtca agcttctgag cgcggtgtcc gggctgaacc gcggcctcgc 60 ggggagccag gaggatcttg accgcgccga cgcggcggcg agggagctcg aggcggcggc 120 gggtggcggc cccgtcgacc tggagaggga cgtggacaag ctgcaggggc ggtggaggct 180 ggtgtacagc agcgcgttct cgtcgcggac gctcggcggc agccgccccg gcccgcccac 240 cggccgcctc ctccccatca ccctcgggca ggtgtttcag aggatcgatg ttgtcagcaa 300 ggacttcgac aacatcgtcg atgtcgagct cggcgcgcca tggccgctgc cgccggtgga 360 gctgacggcg accctggctc acaagtttga gatcatcggc acctcgagca taaagatcac 420 attcgacaag acgacggtga agacgaaggg gaacctgtcc cagctgccgc cgctggaggt 480 ccctcgcatc ccggacaacc tccggccgcc gtccaacacc ggcagcggcg agttcgaggt 540 gacctacctc gacggcgaca cccgcatcac ccgcggggac agaggggagc tcagggtgtt 600 cgtcatctcg tga 613

[0048] Another example of a receptor in accordance with the present invention is found in cotton and has the amino acid sequence of SEQ. ID. No. 6 as follows: MASSSFLLESPASIFSSSSIKAHLYLPKPYPFIVSVKRRRSERKRNPVLK SAVGDVSVVDTPPPPPPPPQDAKSELISSLKLKLLGIVSGLNRGLAANQD DLGKADDAAKELETVAGPVDLLTDLDKLQGRWKLIYSSAFSSRTLGGSRP GLPTGRLLPVTLGQVFQRIDVISKDFDNIAEIELGAPWPLPPLEVTATLA HKFEIIGSSKIKITFEKTSVKTRGTFSQLPSLDVPRIPDALRPPSNPGSG DFDVTFIDADTRITRGDRGELRVFVIS

[0049] This protein, known as GhHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 7 as follows: AAAGCTTTCTTGCAAAAAGCTCCGAAAAAGGGCCAGCAAAAGCCACTTGA GAGCCAATGGCTTCTTCAAGTTTTCTTCTAGAATCTCCGGCGTCTATCTT CTCTTCTTCCTCCATTAAAGCTCATCTCTATCTCCCGAAACCCTACCCTT TTATTGTTAGCGTGAAACGGCGCCGTTCGGAAAGGAAGCGAAACCCTGTT TTAAAATCGGCTGTTGGAGATGTCTCCGTCGTTGACACCCCACCGCCGCC GCCGCCTCCACCTCAAGATGCTAAATCTGAACTCATTTCTTCTTTGAAGC TTAAATTACTGGGTATTGTTTCTGGGCTGAATAGAGGTCTTGCTGCGAAC CAAGATGATCTCGGAAAAGCAGATGATGCCGCCAAGGAACTCGAAACGGT TGCTGGACCTGTGGACTTATTGACCGATCTTGATAAGCTGCAAGGGAGAT GGAAACTGATATACAGCAGTGCATTCTCGTCTCGTACACTCGGCGGGAGC CGTCCTGGACTTCCCACTGGAAGGTTGCTCCCTGTAACTCTCGGCCAGGT TTTTCAGAGAATTGATGTCATAAGCAAAGATTTTGATAATATAGCAGAAA TTGAATTGGGAGCTCCATGGCCATTACCTCCACTTGAAGTTACTGCTACC TTAGCTCACAAATTTGAAATCATAGGATCTTCAAAGATCAAAATAACATT CGAGAAAACGAGTGTGAAAACTAGAGGGACCTTTTCTCAGCTTCCGTCAT TGGATGTACCTCGGATTCCCGACGCTTTGAGGCCTCCATCTAATCCAGGG AGCGGCGACTTTGATGTTACCTTCATTGATGCCGATACCCGAATCACCAG AGGAGATAGAGGTGAGCTTAGGGTTTTTGTCATCTCATAAATTAGTAAGC ACATCTAATATCAAAGCTCGTATGCACTCTCATTACTTCATATATTGTC TGTATGTGTATATATCATTGGGGGTGATCCGTAACTTTTTGTAGAATTAA TATTTTAATGTAATTACGAATATTATGTATGTAAATTTTCGAATCAATTT AATAGTTTAATCGTG

[0050] Another example of a receptor in accordance with the present invention is found in soybean and has the amino acid sequence of SEQ. ID. No. 8 as follows: MASLNLLPHPPLFSSFLHRPHCNTHLLLTPKPSQRRPSLVVKSTVGVADP SPSSSSYAGDTSDSISSLKLNLLSAVSGLNRGLAASEDDLRKADDAAKEL EAAGGLVDLSLGLDNLQGRWKLIYSSAFSSRTLGGSRPGPPIGRLLPITL GQVFQRIDILSKDFDNIVELQLGAPWPLPPLEATATLAHKFELIGSSKIK IVFEKTTVKTAGNLSQLPPLEVPRIPDALRPPSNTGSGEFEVTYLDSDTR ITRGDRGELRVFVIA

[0051] This protein, known as GmHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 9 as follows: GGCACGAGGCTCCAATCCATGGCTTCCCTGAACCTCCTTCCCCACCCTCC ACTTTTCTCTTCTTTCCTTCACAGACCACACTGCAACACCCATCTTCTTC TCACACCAAAACCTTCTCAACGAAGGCCTTCTCTTGTGGTCAAATCTACT GTGGGTGTGGCTGACCCTTCTCCATCTTCTTCTTCCTACGCTGGGGATAC CTCTGATTCCATCTCTTCTTTGAAGCTCAATCTGCTGAGTGCTGTTTCTG GGCTAAATAGAGGCCTTGCTGCAAGCGAAGACGATCTTCGAAAGGCAGAT GATGCTGCTAAGGAACTTGAAGCTGCTGGAGGACTTGTGGATCTCTCGCT TGGTCTTGACAATTTGCAAGGAAGATGGAAACTCATTTATAGCAGCGCAT TTTCGTCTCGAACCCTTGGTGGAAGCCGTCCTGGTCCTCCCATAGGAAGA CTCCTTCCTATTACTCTTGGACAGGTTTTTCAACGAATTGACATCTTGAG CAAAGATTTTGATAACATAGTGGAGCTTCAACTAGGTGCTCCATGGCCCC TACCACCCCTTGAAGCGACTGCCACATTAGCTCACAAATTTGAACTCATA GGATCTTCAAAGATAAAGATAGTATTTGAGAAAACCACTGTGAAGACAGC TGGGAATTTGTCACAGTTGCCACCATTGGAGGTGCCTCGGATTCCCGATG CATTGAGGCCTCCATCTAATACGGGAAGCGGTGAATTTGAAGTTACATAT CTTGACTCGGATACTCGCATCACAAGAGGAGACAGAGGCGAGCTAAGGGT CTTTGTGATTGCTTGAGTTCCTGGTGAATGCAACTATGCACTATGCATTT TCTCTGTTGGACTTAAAAAAAAAAGGTTTCAACACCTTGTGCCATCATTT TGTTTAGTTTTTTCCTCCTGATGGTATTTGTTCTAAGTTCTTCAATATTG TAAACATGATGGAATTAAACTCTACTATATAGTTCCAAGGAAGCAGGGTA CTTTTTGTTTAAGTGTAACATATTTCTTTTTTAAGGAATAATTGCTTACA GATCATTAGATATGGATACTTGAAT

[0052] Another example of a receptor in accordance with the present invention is found in barley and has the amino acid sequence of SEQ. ID. No. 10 as follows: MAMASPSWSSCCTSTSTHSLPGPPASSKGRNPWRASSGRRSASGGKRQQK LSIRAVAAPSAAVDYSDTGAGAGDIPSKIKLLSAVAGLNRGLAASQEDLD RADAAARQLEAAAPAPVDLAKDLDKLQGRWRLVYSSAFSSRTLGGSRPGP PTGRLLPITLGQVFQRIDVVSQDFDNIVELELGAPWPLPPVEATATLAHK FEITGIASIKINFDKTTVKTNGNLSQLPLLEVPRIPDSLRPPTSNTGSGE FNVTYLDDDTRITRGDRGELRVFVVT

[0053] This protein, known as HvHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 11 as follows: GCCGGTCGGCACCCAACTGGAGGTTCAGTTTCCTCGTTGCTCTCCTCCATTGATTGACCGCCTCCTTCC CTGAGGCGCACGGTACACGGACGGCACCCATGGCCATGGCATCGCCGTCGTGGTCATCCTGCTGCACCT CAACCTCCACCCATTCTCTGCCCGGTCCTCCCGCGAGCAGCCAGGGCAGGAACCCGTGGCGGGCAAGCA GCGGCAGGAGGAGCGCCAGCGGAGGGAAGAGGCAGCAGAAGCTGTCCATCCGCGCGGTGGCCGCACCGT CGGCCGCGGTGGACTACTCGGACACCGGCGCCGGCGCCGGCGACATCCCCTCGCTGAAAATCAAGCTGC CGAGCGCCGTCGCCGGGCTGAACCGGGGCCTCGCTGCGAGCCAGGAGGACCTGGACCGGGCGGACGCGG CGGCGCGGCAGCTCGAGGCGGCGGCGCCGGCCCCCGTGGACCTCGCCAAGGATCTCGACAAGCTGCAGG GGCGGTGGAGGCTGGTCTACAGCAGCGCCTTCTCGTCGCGGACGCTCGGCGGCAGCCGCCCCGGCCCGC CCACCGGTCGCCTCCTCCCCATCACCCTCGGCCAGGTGTTCCAGAGGATCGACGTGGTGAGCCAGGACT TCGACAACATCGTGGAGCTCGAGCTCGGCGCCCCGTGGCCGCTGCCGCCGGTGGAGGCCACGGCCACGC TGGCACACAAGTTTGAGATCACCGGAATCGCGAGTATCAAGATCAATTTCGACAAGACGACGGTGAAGA CGAACGGGAACCTGTCCCAGCTGCCGCTGCTGGAGGTGCCCCGCATCCCGGATAGCCTCAGGCCGCCGA CTTCCAACACCGGGAGCGGCGAGTTCAACGTGACCTATCTCGACGACGACACCCGCATCACCCGAGGGG ACAGGGGGGAGCTCAGGGTGTTCGTCGTCACATGAGCTTTTTTTTGCTGCGATCTCTCTCTTTGTAGTG CTCCAACTTTTTTTGGCCCGTAAAACAAGAGTCTTGTACTAGTTCTATATATGCCTTTTGTTTTGGGGT TCACCCGTCCATCCGCGGGAAACATCTATCGTGACGACTGTTCGATGTATAAGCGGAGTCGTCCGATTT ACGCGGTTCCGTCGTCTTTTCGAAC

[0054] Another example of a receptor in accordance with the present invention is found in tomato and has the amino acid sequence of SEQ. ID. No. 12 as follows: MASLLHSRLPLSHNHSLSNSCQSFPCHLPGRSKRSTQRLLEERSYDSKRS LVCQSGIDEVTFIEPPGSKEAEAELIGSLKLKLLSAVSGLNRGLAASEDD LKKADEAAKELESCAGAVDLAADLDKLQGRWKLIYSSAFSSRTLGGSRPG PPTGRLLPITLGQVFQRIDVLSKDFDNIVELELGAPWPFPPVEATATLAH KFELIGSSTIKIIFEKTTVKTTGNLSQLPPLEVPRIPDQFRPPSNTGSGE FEVTYIDSDTRVTRGDRGELRVFVIS

[0055] This protein, known as LeHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 13 as follows: TCGATCCTTTTTCTGAAATTCAAGCTCAACCATGGCTTCTCTACTTCATTCGAGACTTCCCCTTTCTCA CAATCATTCTTTATCAAATTCTTGCCAATCTTTCCCATGTCATCTCCCAGGAAGAAGCAAGAGAAGTAC TCAAAGATTATTAGAGGAAAGGAGCTATGACAGCAAGAGAAGTTTAGTTTGCCAGTCGGGTATTGATGA AGTCACTTTTATTGAGCCACCTGGTAGTAAAGAAGCTGAAGCGGAGCTTATTGGGTCTCTCAAACTCAA GTTATTGAGTGCTGTTTCTGGGCTAAACAGAGGTCTTGCTGCAAGTGAAGATGATCTAAAGAAGGCGGA TGAGGCTGCCAAGGAGCTAGAATCTTGTGCAGGAGCTGTAGATCTCGCAGCTGATCTTGATAAACTTCA AGGGAGGTGGAAATTGATATACAGCAGTGCATTCTCATCTCGTACTCTTGGTGGAAGTCGTCCTGGACC CCCCACTGGAAGACTTCTTCCCATCACTCTTGGTCAGGTATTTCAAAGAATCGATGTACTGAGCAAAGA TTTTGACAACATAGTGGAGCTTGAATTAGGTGCTCCGTGGCCTTTCCCGCCTGTTGAAGCAACTGCCAC TTTAGCCCACAAATTTGAACTTATAGGATCATCTACGATTAAGATTATATTCGAGAAAACTACAGTGAA GACAACTGGAAATTTATCACAGCTCCCACCATTAGAAGTGCCTCGCATACCAGATCAGTTCAGGCCACC ATCAAATACAGGAAGTGGTGAGTTTGAAGTTACCTACATCGATTCTGATACACGAGTAACAAGGGGAGA CAGAGGAGAGCTTAGAGTTTTCGTTATCTCATAAGTTAAGCTGCAATGAATATAGTCTTCCTACAATGT TTTGTTGCTACAATTTCATGTAACAACATATCAAATGTGTAGATATGCTCAACATTATTCTGCTGGTCA CAGCTATCAAATCTGTAATGCTACTGCAAATTCAAATCTGTATACAGTAAATTTGACATC

[0056] Another example of a receptor in accordance with the present invention is found in rice and has the amino acid sequence of SEQ. ID. No. 14 as follows: MAAAVASSCCASTSARPLVRRAGSRNGKLWWAGGVRKARLLSISATAAAP SGVDYAAGTGAAADDDAVAALKVKLLSAVSGLNRGLAGSQEDLDRADAAA RELEAAAGGGPVDLERDVDKLQGRWRLVYSSAFSSRTLGGSRPGPPTGRL LPITLGQVFQRIDVVSKDFDNIVDVELGAPWPLPPVELTATLAHKFEIIG TSSIKITFDKTTVKTKGNLSQLPPLEVPRIPDNLRPPSNTGSGEFEVTYL DGDTRITRGDRGELRVFVIS

[0057] This protein, known as OsHrBP1-1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 15 as follows: TCGCCATTGATTTTCTCTGTCTGCTCTGCTGCTCGCTTGCTTGCGCTGTCCGGTTTAGCTCTGTCTAGC TAGGTAGACTGCGGCCATGGCGGCGGCGGTGGCGTCGTCTTGCTGCGCCTCGACCAGCGCTCGCCCACT GGTTCGCCGCGCCGGGAGCAGGAACGGGAAGCTGTGGTGGGCGGGTGGTGTCAGGAAGGCGCGGCTGCT GTCCATCTCCGCCACGGCCGCGGCGCCGTCGGGCGTGGACTACGCGGCGGGCACCGGCGCCGCCGCCGA CGACGACGCCGTGGCTGCGCTCAAAGTCAAGCTTCTGAGCGCGGTGTCCGGGCTGAACCGCGGCCTCGC GGGGAGCCAGGAGGATCTTGACCGCGCCGACGCGGCGGCGCGGGAGCTCGAGGCGGCGGCGGGTGGCGG CCCCGTCGACCTGGAGAGGGACGTGGACAAGCTGCAGGGGCGGTGGAGGCTGGTGTACAGCAGCGCGTT CTCGTCGCGGACGCTCGGCGGCAGCCGCCCCGGCCCGCCCACCGGCCGCCTCCTCCCCATCACCCTCGG GCAGGTGTTTCAGAGGATCGATGTTGTCAGCAAGGACTTCGACAACATCGTCGATGTCGAGCTCGGCGC GCCATGGCCGCTGCCGCCGGTGGAGCTGACGGCGACCCTGGCTCACAAGTTTGAGATCATCGGCACCTC GAGCATAAAGATCACATTCGACAAGACGACGGTGAAGACGAAGGGGAACCTGTCCCAGCTGCCGCCGCT GGAGGTCCCTCGCATCCCGGACAACCTCCGGCCGCCGTCCAACACCGGCAGCGGCGAGTTCGAGGTGAC CTACCTCGACGGCGACACCCGCATCACCCGCGGGGACAGAGGGGAGCTCAGGGTGTTCGTCATCTCGTG ATCGGACGGACGCGTTCGCGACATAGGTATGCGGCTTGCGATTCTGAAACTGAAACTGAAGCGCACACA CGGTTTTGTGTTCTTTCTCTGCTACTAGTAGATCCTCACTCTCTTGATCTGACCATCTTTGTACTATAC TTCAGTATTGTTCGTGCGTTCTGTATTGTTATAGATTTTGCAGATATTCAACAAGTAGAGGGAAATATG TCAAAATGAGAAATCGAGG

[0058] Another example of a receptor in accordance with the present invention is found in rice and has the amino acid sequence of SEQ. ID. No. 16 as follows: MAAAVASSCCASTSARPLVRRAGSRSGKLWWAGGGRKARLLSISATAAAP SGVDYAAGTGAADDDAVAALKVKLLSAVSGLNRGLAASQEDLDRADAAAR ELEAAAGGGPVDLEGDMDKLQGRWRLVYSSAFSSRTLGGSRPGPPTGRLL PITLGQVFQRIDVVSKDFDNIVDVELGAPWPLPPVELTATLAHKFEIIGT SSIKITFDKTTVKTKGNLSQLPPLEVPRIPDNLRPPSNTGSGEFEVTYLD GDTRITRGDRGELRVFVIS

[0059] This protein, known as OsHrBP1-2p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 17 as follows: TCGCCATTGATTTTCTCTGTCTGCTCTGCTGCTCGCTTGCTTGCGCTGTCCGGTTTAGCTCTGTCTAGC TAGGTAGACTGGCGGCCATGGCGGCGGCGGTGGCGTCGTCTTGCTGCGCCTCGACCAGCGCTCGCCCAC TGGTTCGCCGCGCCGGGAGCAGGAGCGGGAAGCTGTGGTGGGCGGGTGGTGGGAGGAAGGCGCGGCTGC TGTCCATCTCCGCCACGGCCGCGGCGCCGTCGGGCGTGGACTACGCGGCGGGCACCGGCGCCGCCGACG ACGACGCCGTGGCTGCGCTCAAAGTCAAGCTTCTGAGCGCGGTGTCCGGGCTGAACCGCGGCCTCGCGG CGAGCCAGGAGGATCTTGACCGGGCCGACGCGGCGGCGCGGGAGCTCGAGGCGGCGGCGGGCGGCGGGC CCGTCGACCTGGAGGGGGACATGGACAAGCTGCAGGGGCGGTGGAGGCTGGTGTACAGCAGCGCGTTCT CGTCGCGGACGCTCGGCGGCAGCCGCCCCGGCCCGCCCACCGGCCGCCTCCTCCCCATCACCCTCGGCC AGGTGTTTCAGAGGATCGATGTTGTCAGCAAGGACTTCGACAACATCGTCGATGTCGAGCTCGGCGCGC CATGGCCGCTGCCGCCGGTGGAGCTGACGGCGACGCTGGCTCACAAGTTTGAGATCATCGGCACCTCGA GCATAAAGATCACATTCGACAAGACGACGGTGAAGACGAAGGGGAACCTGTCCCAGCTGCCGCCGCTGG AGGTCCCTCGCATCCCGGACAACCTCCGGCCGCCGTCCAACACCGGCAGCGGCGAGTTCGAGGTGACCT ACCTCGACGGCGACACCCGCATCACCCGCGGGGACAGAGGGGAGCTCAGGGTGTTCGTCATCTCGTGAT CGGACGGACGCGTTCGCGACATAGGTATGCGGCTTGCGATTCTGAAACTGAAACTGAAGCGCACACACG GTTTTGTGTTCTTTCTCTGCTACTAGTAGATCCTCACTCTCTTGATCTGACCATCTTTGTACTATACTT CAGTATTGTTCGTGCGTTCTGTATTGTTATAGATTTTGCAGATATTCAACAAGTAGAGGGAAATATGCC AAAATGAG

[0060] Another example of a receptor in accordance with the present invention is found in potato and has the amino acid sequence of SEQ. ID. No. 18 as follows: MASLLHSRLPLSHNHSLSNSCQSFPCHLPGRSKRSTQRFFEERSYDSKRA LICQSGIDEVTFRLPGSKEAKAELIGSLKLKLLSAVSGLNRGLAASEDDL KKADEAAKELESCAGAVDLAADLDKLQGRWKLIYSSAFSSRTLGGSRPGP PTGRLLPITLGQVFQRIDVLSKDFDNIVELELGAPWPFPPVEATATLAHK FELIGSSTIKIVFEKTTVKTTGNLSQLPPIEVPRIPDQFRPPSNTGNGEF EVTYIDSDTRVTRGDRGELRVFVIS

[0061] This protein, known as StHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 19 as follows: CTACCACCAATCAAACTCCACAAAAGATCGATCCTTTTTCTGAAATTCAAGCTCAACCATGGCTTCTCT ACTTCATTCTAGACTTCCCCTTTCTCACAATCATTCTTTATCAAATTCTTGCCAATCTTTCCCCTGTCA TCTCCCAGGAAGAAGCAAGAGAAGTACTCAAAGATTCTTTGAGGAAAGGAGCTATGATAGCAAGAGAGC CTTAATTTGTCAGTCGGGTATTGATGAAGTCACTTTTAGGCTACCTGGTAGTAAAGAAGCTAAAGCTGA GCTTATTGGGTCTCTCAAACTCAAGTTATTGAGTGCTGTTTCTGGGCTAAACAGAGGTCTTGCTGCAAG TGAAGATGATCTAAAGAAGGCGGATGAGGCTGCCAAGGAGCTGGAATCTTGTGCAGGAGCTGTAGATCT CGCAGCTGATCTTGATAAGCTTCAAGGGAGGTGGAAATTGATATACAGCAGTGCATTCTCATCTCGTAC TCTTGGTGGAAGTCGTCCTGGCCCCCCCACTGGAAGACTTCTTCCCATCACTCTTGGTCAGGTATTTCA AAGAATTGATGTACTAAGCAAGGATTTTGACAACATAGTGGAGCTTGAATTAGGTGCTCCGTGGCCTTT CCCACCTGTTGAAGCAACTGCCACTTTAGCCCACAAATTTGAACTTATAGGATCATCTACAATTAAGAT TGTATTCGAAAAACTCAGTGAAGACAACTGGAAATTTATCACAGTTGCCACCAATAGAAGTGCCTCCAT ACCAGATCAGTTCAGGCCACCATCAAATACAGGAAATGGTGAGTTTGAAGTTACCTATATCGATTCTGA TACACGTGTAACAAGGGGAGACAGAGGAGAGCTTAGAGTTTTCGTTATCTCATAAGTTAAGCTGCAATA AATATAGTTTTCCTACAATATTTTGTTGCTACAATTTCATGTAACAACATATCNAATGTATAGATATGC TCAACATTATTCTGCTGGTCAAAGCTAGCAAATTTGTAATGCTACTGCAAATTCAAATCTGTATACAGT AAATTTGACATGTGATGGAGTTATGCAGTGAGATTTCNANAAT

[0062] Another example of a receptor in accordance with the present invention is found in wheat and has the amino acid sequence of SEQ. ID. No. 20 as follows: MAMASPSWSSCCASTSTRPLPSPPASSKSRNPWRASSGRRSASGGKRRQQ LSIRAVAAPSSAVDYSDTAAGAGDVPSLKIKLLSAVAGLNRGLAASQEDL DRADAAARQLEAAAPAPVDLAKDLDKLQGRWLVYSSAFSSRTLGGSRPGP PTGRLLPLITLGQVFQRIDVVSQDFDNIVELELGAPWPLPPVEATATLAH KFEITGIASIKINFDKTTVKTKGNLSQLPLLEVPRIPDSLRPTTSNTGSG EFDVTYLDDGTRITRGDRGELRVFVVS

[0063] This protein, known as TaHrBP1-1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 21 as follows: GAATTCGGCACGAGCTGACCTCTTGCCGGTCGGCGCCCAATTGAAAATTT CTTTTCTTTTTGCTCTCCTGATCGATTGACTGCCTCACGGACGGTGCCCA TGGCCATGGCATCGCCGTCGTGGTCATCTTGCTGCGCCTCCACCTCCACC CGTCCTCTGCCTAGCCCCCCCGCGAGCAGCAAGAGCAGGAACCCATGGCG GGCAAGCAGCGGCAGGAGGAGCGCCAGCGGAGGGAAGAGACGACAGCAGC TGTCCATCCGCGCGGTGGCCGCACCGTCGTCGGCGGTGGACTACTCGGAC ACCGCCGCCGGCGCCGGCGACGTCCCCTCGCTGAAAATCAAGCTGCTGAG CGCGGTCGCCGGGCTGAACCGGGGCCTCGCGGCGAGCCAGGAGGACCTGG ACCGGGCGGACGCGGCGGCGAGGCAGCTCGAGGCGGCGGCACCGGCCCCC GTGGACCTCGCCAAGGACCTCGACAAGCTGCAGGGGCGGTGGAGGCTGGT CTACAGCAGCGCCTTCTCGTCGCGGACGCTCGGCGGCAGCCGCCCCGGCC CGCCCACCGGCCGCCTCCTCCCCATCACCCTCGGCCAGGTGTTCCAGAGG ATCGACGTGGTCAGCCAGGACTTCGACAACATCGTGGAGCTCGAGCTCGG CGCGCCGTGGCCGCTGCCGCCGGTCGAGGCCACGGCCACGCTGGCGCACA AGTTTGAGATCACCGGAATCGCGAGTATCAAGATCAATTTCGACAAGACG ACGGTGAAGACCAAAGGGAACCTGTCCCAGCTGCCTCTGCTGGAGGTGCC CCGCATCCCGGATAGCCTCCGGCCTACGACGTCCAACACCGGGAGCGGCG AGTTCGACGTGACCTACCTCGACGACGGCACCCGCATCACCCGAGGGGAC AGGGGGGAGCTCAGGGTGTTCGTCGTCTCATGAGCTGATATTTTTTTTGT TGATGTTGCTGCTGCTTTCTCTCTCCGTGTACTGCTTCAACCTTTTTGCC CCTAAACAGAAGTCTTGAACTAGTTCTATGTCTATTTTTGCCGGAGTAGT ATCGTG

[0064] Another example of a receptor in accordance with the present invention is found in wheat and has the amino acid sequence of SEQ. ID. No. 22 as follows: MAAPSWSSCCASTSTRPLPSPPASSKGGNPWRASSGRRSASGGKRQQQLS IRAVAAPSSAVDYSDTGAGAADVPSLKIKLLSAVAGLNRGLAASQEDLDR ADAAARQLEAAAPAPVDLAKDLDKLQGRWRLVYSSAFSSRTLGGSRPGPP TGRLLPITLGQVFQRIDVVSQDFDNIVELELGAPWPLPPVEATATLAHKF EITGIASIKINFDETTVKTNGNLSQLPLLEVPRIPDSLRPPASNTGSGEF DVTYLDDDTRITRGDRGELRVFVIA

[0065] This protein, known as TaHrBP1-2p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 23 as follows: ACTAGTGATTCGCGGATCCATATGCTGCGTTTGCTGGCTTTGATGAAACT CGTGCTCGTCTCTGACCTCTGGCCGGTCGGCACCCAACTGAAAATATCTT TTCTCGTTGCTCTCCTCGATCGATTGACTGCTTCACCGGACGGTGCCCGT GGCCATGGCAGCGCCGTCGTGGTCATCTTGCTGCGCCTCCACCTCCACCC GTCCTCTGCCTAGCCCTCCCGCGAGCAGCAAGGGCGGGAACCCATGGCGG GCAAGCAGCGGCAGGAGGAGCGCCAGCGGAGGGAAGAGGCAGCAGCAGCT GTCCATCCGCGCGGTGGCCGCGCCGTCGTCGGCGGTGGACTACTCGGACA CCGGCGCCGGCGCCGGCGACGTCCCCTCGCTGAAAATCAAGCTGCTGAGC GCGGTGGCCGGGCTGAACCGGGGCCTCGCGGCGAGCCAGGAGGACCTGGA CCGGGCGGACGCGGCGGCGAGGCAGCTCGAGGCGGCGGCGCCGGCCCCCG TGGACCTCGCCAAGGACCTCGACAAGCTGCAGGGGCGGTGGAGGCTGGTC TACAGCAGCGCCTTCTCGTCGCGGACGCTCGGCGGTAGCCGCCCCGGCCC GCCCACCGGCCGCCTGCTCCCCATCACCCTCGGCCAGGTGTTCCAGAGGA TCGACGTGGTGAGCCAGGACTTCGACAACATCGTGGAGCTCGAGCTCGGC GCGCCGTGGCCGCTGCCGCCGGTGGAGGCCACGGCCACGCTGGCACACAA GTTTGAGATCACCGGGATCGCGAGTATCAAGATCAATTTCGACGAGACGA CGGTGAAGACGAATGGGAACCTGTCCCAGCTGCCTCTGCTGGAGGTGCCC CGCATCCCGGATAGCCTCCGGCCGCCGGCGTCCAACACCGGGAGCGGCGA GTTCGACGTGACCTACCTCGACGACGACACCCGCATCACCCGAGGGGACA GGGGGGAGCTCAGGGTGTTCGTCATCGCATGAGCTTGATCTTTGCTTGAG ATCTCTGTCTCTGTACTGCTTCACTTTTTTTGCCCCGAAACAGAAGTCTT TGTCTAGTTCTATGTCTTCTTTTGCCGGCGTAGTATTGTGATATAGGCTA ACGTGCGTTCTTCACCTATGGGATTAACTTTTTCTCTCTAGCAGATTATT ACGTCCGGTTATTTCGTTTTGGTTTTATTATGTTGGCTTAAGTTTTAATT ATGTG

[0066] Another example of a receptor in accordance with the present invention is found in maize and has the amino acid sequence of SEQ. ID. No. 24 as follows: MAATWSSSCCAATASSSALLRHARVKSAPWVAGASRSSYRQRRRRRELSI RATAAAPPPPVVYADAGADNVASLKIKLLSAVSGLNRGLAASQEDLDRAD AAARELEAAAGCPVDLSRDLDKLQGRWRLLYSSAFSSRTLGGSRPGPPTG RLLPITLGQVFQRIDVVSRDFDNIVELELGAPWPLPPLEATATLAHKFEI IGTSGIKITFEKTTVKTKGNLSQLPPLEVPRIPDNLRPPSNTGSGEFEVT YLDDDTRVTRGDRGELRVFVIA

[0067] This protein, known as ZmHrBP1p, is encoded by a cDNA molecule which has a partial sequence corresponding to SEQ. ID. No. 25 as follows: CCACCACAAATATTCTTCCCGCCACGATCCCTCTCATCCGGAAGAAAGGG GAAAAAAACTCGCCTTTTTCTCTCTGCTGGTTCAAGAACGCCATGGAAGA TCTCGAGCGCTCGCTGTGATTCCTGCGAGTACCCAAGCCCAACCAAGCCC TGGCCCGGCAGCCATTCTCTTCGCGCCACATCGCACGACCTCCCCGAAGC AGACGTGCCCGCTGCCCGTCCGTCCCCCGTGGCCATGGCCGCGACGTGGT CTTCGTCTTGCTGCGCCGCGACCGCGTCGAGCAGCGCTCTGCTTCGTCAT GCCCGCGTCAAGAGCGCGCCTTGGGTAGCCGGTGCCAGCCGGAGTAGCTA CAGGCAGCGGCGGCGGCGGCGGGAGCTGTCCATCCGCGCCACGGCCGCGG CGCCGCCGCCGCCCGTGGTCTACGCGGACGCCGGCGCCGACAACGTGGCC TCGCTGAAGATCAAGCTCCTGAGCGCGGTGTCCGGGCTGAACCGTGGCCT GGCAGCGAGCCAGGAGGACCTGGACCGCGCGGACGCGGCGGCGCGGGAGC TGGAGGCGGCGGCGGGGTGCCCCGTCGACCTCAGCAGGGACCTCGATAAG CTGCAGGGCCGGTGGCGGCTGCTGTACAGCAGCGCGTTCTCTTCGCGGAC GCTCGGCGGCAGCCGCCTTGGCCCGCCCACCGGCCGCCTCCTCCCCATCA CGCTCGGCCAGGTGTTCCAGCGGATCGACGTGGTGAGCCGCGACTTCGAC AACATCGTGGAGCTGGAGCTCGGCGCGCCGTGGCCTCTGCCGCCGCTCGA GGCCACGGCGACGCTGGCGCACAAGTTCGAGATCATCGGGACCTCGGGCA TCAAGATCACGTTCGAGAAGACGACGGTGAAGACCAAGGGCAACCTGTCG CAGCTTCCTCCGCTGGAGGTGCCCCGCATCCCCGACAACCTCCGCCCCCC GTCCAACACCGGGAGCGGCGAGTTCGAGGTGACCTACCTCGACGACGACA CGCGCGTCACCCGCGGGGACAGGGGGGAGCTCAGGGTGTTTGTCATCGCG TGACCTGATCGCGCTTCGGCGCCGTTCTGCTGGTCCGTGAGATTGCCATC CTTCTTCCTCCCTGTTGCTCCAGTAGATTTGTTGGTTTCTTCGTCTGACC AATGTATACCGTTCTGTTCTTCCGTGAACTGAATCTGCGATTAACTTAGT AACTATCTTGTGTGGTTT

[0068] Another example of a receptor in accordance with the present invention is found in grapefruit and has an amino acid sequence of SEQ. ID. No. 26 as follows: MASLTLTPLFHSPTFLSSNTNTHTVTKKLSFPSPTRRRLLVNGKEYRSRR RSLVLRRSAVDDVPVLDPPPPPPPDSSESDKTELIASLKLKLLSAVSGLN RGLAANTDDLQKADAAAKELEAVGGPVDLSVGLDRLQGKWRLLYSSAFSS RTLGGNRPGPPTGRLLPITLGQVFQRIDILSKDFDNIAELELGVPWPLPP VEVTATLAHKFELIGSSNIKIIFEKTTVKTTGNLSQLPPLELPRFPDALR RPSDTRSGEFEVTYLDNDTRITRGDRGELRVFVIT

[0069] This protein, known as CpHrBP1p, is encoded by a cDNA molecule which has a sequence corresponding to SEQ. ID. No. 27 a follows: TTCGATTGCCAGACGCTGCGTTTGCTGGCTTTGATGAAACCTCTTTCATT CCCTGCTGGCCACAAACACACGCCGACATTGAAACTCCCCCCACCCACAT CATGGCTTCTCTGACTCTAACCCCTCTTTTTCATTCACCAACATTTCTTT CCAGCAATACTAACACACACACAGTCACAAAAAAACTGTCTTTTCCATCT CCAACGCGACGTCGTCTGCTTGTTAATGGTAAGAGTATCGAAGTAGAAGA AGAAGCCTTGTTTTGAGGAGGTCAGCCGTTGATGACGTTCCTGTTCTTGA CCCACCACTCCTCCTCCTCCCGATTCTTCAGAAAGCGACAAAACTGAGCT CATTGCTTCTTTGAAGCTCAAGTTGCTTAGTGCTGTTTCTGGGCTGAACA GAGGTCTTGCTGCAAACACAGATGATCTGCAGAAGGCAGACGCTGCTGCA AAAGAGCTTGAGGCTGTTGGAGGACCAGTAGACCTCTCGGTTGGTCTCGA TAGACTACAAGGGAAATGGAGACTACTGTACAGCAGTGCATTCTCATCTC GCACTCTAGGTGGAAATCGGCCTGGACCTCCCACTGGAAGGCTACTCCCC ATAACTCTTGGCCAGGTCTTTCAACGGATTGACATCTTAAGCAAAGATTT TGATAACATAGCAGAACTTGAATTGGGTGTTCCATGGCCCCTGCCACCAG TTGAAGTGACTGCCACATTAGCCCATAAATTTGAACTCATAGGATCATCA AATATTAAAATAATATTTGAGAAGACAACTGTAAAGACAACAGGGAACTT ATCACAGCTTCCACCCCTTGAGTTACCTCGTTTTCCAGATGCATTAAGGC GTCCATCTGACACAAGAAGTGGTGAATTTGAGGTGACATACCTCGATAAT GATACCCGCATTACCAGAGGAGACAGAGGCGAGCTAAGAGTTTTCGTGAT CACTTAGGTTCCTTACATCCGTACAGTTTCCAGCTTGTATCTACATTATT TTCTGATGATTATATACACAAAGTGGTAAAAAGAAGCCCCGTGAAAAGCA GTTCTTCCTGGATCAAGTGAATCATTGCACAATTATATATTTTTCATGCG C

[0070] Another example of a receptor in accordance with the present invention is found in apple and has an amino acid sequence of SEQ. ID. No. 28 as follows: MAMASLSSLPHSLHSSPSTSSANYVIPSKPPCPKRLRFGSSNRRHTKSFA PRAAVDEVSVLEPPPPQPPSSGSKTTPNPELVASLKLNLLSAVSGLNRGL AASGEDLQKAEAAAKEIEAAGGPVDLSTDLDKLQGRWKLIYSSAFSSRTL GGSRPGPPTGRLLPITLGQVFQRIDIFSKDFDNIVELELGAPWPLPPVEA TATLAHKFELIGSSRVKIIFEKTTVKTTGNLSQLPPLELPKLPEGLRPPS NPGSGEFDVTYLDADIRITRGDRDELRVFVVS

[0071] This protein, known as MdHrBP1p is encoded by a cDNA molecule which has a sequence corresponding to SEQ. ID. No. 29 a follows: GGCTTTGATGAAATTTCCTTTCTACTTTCTAGCCATGGCCATGGCTTCTT TGAGCTCTCTCCCTCACTCTCTACATTCCTCGCCTTCTACTTCTTCTGCA AACTATGTTATTCCAAGCAAACCACCCTGCCCAAAACGCCTCCGTTTTGG TTCGTCAAATCGCCGTCACACCAAAAGCTTTGCTCCGAGAGCAGCTGTGG ACGAGGTTTCTGTTCTCGAACCGCCGCCACCACAGCCGCCGTCTTCCGGA AGCAAAACCACGCCCAACCCTGAACTTGTAGCGTCTTTAAAGCTCAACCT ATTGAGTGCTGTTTCTGGGCTAAATAGAGGTCTTGCAGCATCGGGAGAGG ATCTACAAAAGGCAGAAGCTGCTGCCAAGGAGATTGAAGCTGCTGGAGGT CCAGTGGATCTCTCAACTGATCTTGATAAACTGCAAGGGAGATGGAAATT GATATATAGCAGTGCATTTTCTTCTCGTACTCTAGGTGGGAGCCGTCCTG GACCTCCCACCGGAAGGCTACTCCCAATTACCTTAGGCCAGGTATTTCAA CGGATTGACATCTTCAGCAAAGACTTTGATAACATAGTGGAGCTTGAACT AGGTGCTCCATGGCCCCTGCCACCCGTTGAAGCAACTGCCACTTTGGCCC ACAAATTTGAACTCATAGGATCTTCCAGGGTTAAGATCATTTTTGAGAAA ACTACTGTGAAGACTACTGGAAACTTATCGCAGCTTCCTCCATTAGAGTT ACCTAAGTTACCGGAAGGACTACGACCTCCGTCTAACCCAGGAAGTGGTG AATTTGACGTTACCTACCTTGATGCTGATATCCGCATCACAAGAGGAGAT AGAGACGAGCTAAGGGTTTTTGTTGTTTCATAGTTTCTTGTTAGTTTCTT TTCCTACTTCCAATGTATCTCCATCTGTTTTGCCTTGCGTCTTCTTGGTG TCGTTTGATCATATGTTGTTACTTCCAATTGTTGTATGCATGAACCGGTG GATGGAAGTTCCAGGAAATGTTCAACGAGGAACAACACTGTATACATGTA AATTTTGTAATCGATAAAGTGAATCGTCTTTGTCACTTGGATTGTATCTG CATTGCCTTTTCAAGTGATATCTATATGAGTTTTAGGC

[0072] Another example of a receptor in accordance with the present invention is found in tobacco and has an amino acid sequence of SEQ. ID. No. 30 as follows: MASLLQYSTLPLSNNHCSSSLPSLTCHLSKRSNRNTQKLLEKKKYHIKKS LICQSGIDELAFIELPGTKEAKAELIGSLKLKLLSAVSGLNRGLAASEED LKKADAAAKELESCAGAVDLSADLDKLQGRWKLIYSSAFSGRTLGGSRPG PPTGRLLPITLGQVFQRIDVLSKDFDNIVELELGAPWPLPPAELTATLAH KFELIGSSTIKITFEKTTVKTTGILSQLPPFEVPRIPDQLRPPSNTGSGE FEVTYIDSDTRVTRGDRGELRVFVIS

[0073] This protein, known as NtHrBP1p, is encoded by a cDNA molecule which has a sequence corresponding to SEQ. ID. No. 31 a follows: ATTCACAAACCTTTCCAAATATTGAGCTGAAATTAAAGCTCAACAATGGCTTCTCTACTTCAGTACTCT ACACTTCCTCTTTCTAATAATCATTGTTCATCTTCGTTACCATCTTTAACTTGTCATCTCTCAAAAAGA AGCAATAGAAATACTCAAAAATTATTAGAGAAAAAGAAGTATCATATCAAGAAAAGCTTAATTTGCCAG TCGGGTATTGATGAACTCGCATTCATTGAGTTACCTGGTACTAAAGAAGCTAAAGCTGAACTTATTGGG TCTCTCAAACTCAAGTTATTGAGTGCTGTTTCTGGGCTAAACAGAGGTCTTGCTGCGAGCGAAGAAGAC CTAAAGAAGGCGGATGCTGCTGCCAAGGAGCTAGAATCCTGTGCAGGAGCTGTAGATCTCTCAGCTGAT CTCGATAAACTTCAAGGGAGGTGGAAATTGATATACAGCAGTGCATTCTCAGGTCGCACTCTTGGAGGA AGTCGTCCTGGACCCCCCACCGGAAGACTTCTTCCCATTACTCTTGGTCAGGTATTTCAAAGAATTGAT GTGCTAAGCAAGGATTTTGACAACATAGTGGAGCTTGAATTAGGTGCTCCTTGGCCTTTACCACCTGCT GAGTTGACTGCCACTTTAGCCCACAAATTTGAACTGATAGGATCATCCACGATTAAGATTACATTCGAG AAAACTACTGTGAAGACAACCGGAATCTTATCACAGCTCCCACCATTTGAGGTGCCTCGGATACCAGAT CAACTCAGGCCACCATCTAATACAGGAAGTGGTGAGTTTGAAGTTACCTATATTGATTCTGATACACGC GTAACAAGGGGAGACAGAGGAGAGCTTAGAGTTTTCGTTATCTCATAAGATGGAATGCAATAGATATAG TTTTCCTACAATATTTTGTTGCTACAATTTCATGTACAATATATCAAATGTATAGATATGCTCAACATT ATTCTGCTGGTCCATATCTAGCAAAGTTGTAATGTTACTGCAAATTTGAATCTGTATACAGTAAACTCG ATTTTGCGA

[0074] Another example of a receptor in accordance with the present invention is found in grape and has an amino acid sequence of SEQ. ID. No. 32 as follows: MTSLLHPLTSFSLSPSPPPPLSSSSSSTITITCALPSNLRSSDRRRLRTT SKPYTWTSGLPKRSFVLRSTLDEVSVLDPPPPPEDSTADLLSSLKLKLLS AVSGLNRGLAAIEDDLQKADAAAKELEAAGGTVDLSIDLDKLQGRWKLIY SSAFSSRTLGGSRPGPPTGRLLPITLGQVFQRIDIVSKDFDNIVDLQIGV PWPLPPIELTATLAHKFELIGTSSIKITFEKTTVKTTGNLSQLPPLEVPR IPDALRPPSNTGSGEFEVTYLDADTRITRGDRGELRVFVIA

[0075] This protein, known as VsHrBP1-1p, is encoded by a cDNA molecule which has a sequence corresponding to SEQ. ID. No. 33 a follows: ACCGCCAGCCAACTATGACTTCTCTCCTCCATCCTCTCACCTCTTTCTCCCTTTCTCCATCACCACCAC CGCCCCTTTCTTCTTCTTCTTCTTCTACTATTACTATCACGTGTGCTCTTCCCAGTAACCTACGTTCTT CAGACCGACGTCGTCTTAGAACAACATCAAAACCTTATACGTGGACATCGGGCCTGCCCAAGAGAAGCT TTGTCCTGAGGTCAACCCTTGATGAGGTCTCTGTTCTTGACCCCCCTCCTCCCCCTGAAGACTCCACGG CCGATCTTCTTTCGTCTCTCAAGCTGAAACTACTGAGTGCTGTGTCTGGTCTAAATAGAGGACTTGCTG CAATCGAGGATGATCTTCAGAAGGCAGATGCTGCTGCCAAAGAGCTTGAAGCTGCTGGAGGAACTGTTG ACCTCTCAATTGATCTTGATAAACTTCAGGGAAGATGGAAATTGATATATAGCAGTGCGTTCTCATCCC GTACTCTAGGTGGGAGCCGTCCTGGACCTCCCACTGGAAGGCTACTCCCTATAACTCTGGGCCAGGTAT TTCAAAGGATTGACATTGTAAGCAAAGATTTTGACAATATAGTAGATCTCCAGATAGGTGTCCCATGGC CCCTTCCGCCAATTGAACTCACTGCCACATTAGCCCACAAGTTTGAACTCATAGGAACTTCCAGCATTA AAATAACATTCGAGAAAACAACTGTGAAGACAACAGGAAACCTGTCGCAGCTGCCACCATTGGAGGTAC CTCGGATCCCAGATGCATTGAGGCCACCATCTAATACAGGAAGTGGCGAATTTGAGGTTACATACCTTG ATGCTGATACCCGCATCACCAGAGGAGACAGGGGTGAGCTTAGAGTTTTTGTCATTGCATAAACTCTAA GCACTCGTCACCATGACTCACAATTGAAGAAAATACCATATCCAATCCCCTTTTCTTCTTGTCATTTTG TAAACAGTCCCCTGTTTCTTACTGTTTGTAGGGAACATGTCTTGTTACATATAACTGTAAATTCATTTT TTT

[0076] Another example of a receptor in accordance with the present invention is found in grape and has an amino acid sequence of SEQ. ID. No. 34 as follows: MTSLLHPLTSFSLSPSPPPPLSFSSSSSTITITCALPSNLRSSDRRRLRT TSKPYTWTSGLPKRSFVLRSTLDEVSVLDPPPPPEDSTADLLSSLKLKLL STVSGLNRGLAAIEDDLQKADAAAKELEAAGGTVDLSIDLDKLQGRWKLI YSSAFSSRTLGGSRPGPPTGRLLPITLGQVFQRIDIVSKDFDNIVDLQIG APWPLPPIELTATLAHKFELIGTSSIKITFEKTTVKTTGNLSQLPPLEVP RIPDALRPPSNTGSGEFEVTYLDADTRITRGDRGELRVFVIA

[0077] This protein, known as VsHrBP1-2p, is encoded by a cDNA molecule which has a sequence corresponding to SEQ. ID. No. 35 a follows: ACCGCCAGCCAACTATGACTTCTCTCCTCCATCCTCTCACCTCTTTCTCCCTTTCTCCATCACCACCAC CGCCCCTTTCTTTTTCTTCTTCTTCTTCTACTATTACTATCACGTGTGCTCTTCCCAGTAACCTACGTT CTTCAGACCGACGTCGTCTTAGAACAACATCAAAACCTTATACGTGGACATCGGGCCTGCCCAAGAGAA GCTTTGTCCTGAGGTCAACCCTTGATGAGGTCTCTGTTCTTGACCCCCCTCCTCCCCCTGAAGACTCCA CGGCCGATCTTCTTTCGTCTCTCAAACTGAAACTACTGAGTACTGTGTCTGGTCTAAATAGAGGACTTG CTGCAATCGAGGATGATCTTCAGAAGGCAGATGCTGCTGCCAAAGAGCTTGAAGCTGCTGGAGGAACTG TTGACCTCTCAATTGATCTTGATAAACTTCAGGGAAGATGGAAATTGATATATAGCAGTGCGTTCTCAT CCCGTACTCTAGGTGGGAGCCGTCCTGGACCTCCCACTGGAAGGCTACTCCCTATAACTCTGGGGCAGG TATTTCAAAGGATTGACATTGTAAGCAAAGATTTTGACAATATAGTAGATCTCCAGATAGGTGCCCCAT GGCCCCTTCCGCCAATTGAACTCACTGCCACATTAGCCCACAAGTTTGAACTCATAGGAACTTCCAGCA TTAAAATAACATTCGAGAAAACAACTGTGAAGACAACAGGAAACCTGTCGCAGCTTCCACCATTGGAGG TACCTCGGATCCCAGATGCATTGAGGCCACCATCTAATACAGGAAGTGGCGAATTTGAGGTTACATACC TTGATGCTGATACCCGCATCACCAGAGGAGACAGGGGTGAGCTTAGAGTTTTTGTCATTGCATAAACTC TACACTCGTCACCATGACTCACAATTGAAGAAAATACAATATCCAATCCCCTTTTCTTCTTGTCATTTT GTAAACTGTCCCCTGTTTCTTACTGTTTGTAGGGAACATGTCTTGTTACATAACTGTAAATTCATTTTT TCTACATTTGATCTTTACAG

[0078] Hypersensitive response elicitors recognized by the receptors of the present invention are able to elicit local necrosis in plant tissue contacted by the elicitor.

[0079] Examples of suitable bacterial sources of hypersensitive response elicitor polypeptides or proteins include Erwinia, Pseudomonas, and Xanthamonas species (e.g., the following bacteria: Erwinia amylovora, Erwinia chiysanthemi, Erwinia stewartii, Erwinia carotovora, Pseudomonas syringae, Pseudomonas solanacearum, Xanthomonas campestris, and mixtures thereof).

[0080] An example of a fungal source of a hypersensitive response elicitor protein or polypeptide is Phytophthora. Suitable species of Phytophthora include Phytophthora parasitica, Phytophthora cryptogea, Phytophthora cinnamomi, Phytophthora capsici, Phytophthora megasperma, and Phytophthora citrophthora.

[0081] The hypersensitive response elicitor polypeptide or protein from Erwinia chrysanthemi is disclosed in U.S. Pat. No. 5,850,015 and U.S. Pat. No. 6,001,959, which are hereby incorporated by reference. This hypersensitive response elicitor polypeptide or protein has a molecular weight of 34 kDa, is heat stable, has a glycine content of greater than 16%, and contains substantially no cysteine.

[0082] The hypersensitive response elicitor polypeptide or protein derived from Erwinia amylovora has a molecular weight of about 39 kDa, has a p1 of approximately 4.3, and is heat stable at 100° C. for at least 10 minutes. This hypersensitive response elicitor polypeptide or protein has a glycine content of greater than 21% and contains substantially no cysteine. The hypersensitive response elicitor polypeptide or protein derived from Erwinia amylovora is more fully described in U.S. Pat. No. 5,849,868 to Beer and Wei, Z. -M., et al., “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85-88 (1992), which are hereby incorporated by reference.

[0083] The hypersensitive response elicitor polypeptide or protein derived from Pseudomonas syringae has a molecular weight of 34-35 kDa. It is rich in glycine (about 13.5%) and lacks cysteine and tyrosine. Further information about the hypersensitive response elicitor derived from Pseudomonas syringae and its encoding DNA molecule is found in U.S. Pat. Nos. 5,708,139 and 5,858,786 and He et al., “Pseudomonas syringae pv. syringae Harpin_(pss): A Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants,” Cell 73:1255-66 (1993), which are hereby incorporated by reference.

[0084] The hypersensitive response elicitor polypeptide or protein derived from Pseudomonas solanacearum is set forth in Arlat, M., F. Van Gijsegeem, J. C. Huet, J. C. Pemollet, and C. A. Boucher, “PopA1, a Protein which Induces a Hypersensitive-like Response in Specific Petunia Genotypes, is Secreted via the Hrp Pathway of Pseudomonas solanacearum,” EMBO J. 13:543-533 (1994), which is hereby incorporated by reference. This protein has 344 amino acids, a molecular weight of 33.2 kDa, and a pI of 4.16, is heat stable and glycine rich (20.6%).

[0085] The hypersensitive response elicitor polypeptide or protein from Xanthomonas campestris pv. glycines has a partial amino acid sequence corresponding to SEQ. ID. No. 36 follows: Thr Leu Ile Glu Leu Met Ile Val Val Ala Ile Ile   1               5                  10 Ala Ile Leu Ala Ale Ile Ala Leu Pro Ala Tyr Gln          15                  20 Asp Tyr  25

[0086] This sequence is an amino terminal sequence having only 26 residues from the hypersensitive response elicitor polypeptide or protein of Xanthomonas campestris pv. glycines. It matches with fimbrial subunit proteins determined in other Xanthomonas campestris pathovars.

[0087] The hypersensitive response elicitor polypeptide or protein from Xanthomonas campestris pv. pelargonii is heat stable, protease sensitive, and has a molecular weight of 12 kDa. It has the amino acid sequence of SEQ. ID. No. 37 as follows: Met Asp Ser Ile Gly Asn Asn Phe Ser Asn Ile Gly   1              5                  10 Asn Leu Gln Thr Met Gly Ile Gly Pro Gln Gln His          15                  20 Glu Asp Ser Ser Gln Gln Ser Pro Ser Ala Gly Ser  25                  30                  35 Glu Gln Gln Leu Asp Gln Leu Leu Ala Met Phe Ile              40                  45 Met Met Met Leu Gln Gln Ser Gln Gly Ser Asp Ala      50                  55                  60 Asn Gln Glu Cys Gly Asn Glu Gln Pro Gln Asn Gly  65                  70 Gln Gln Glu Gly Leu Ser Pro Leu Thr Gln Met Leu          75                  80 Met Gln Ile Val Met Gln Len Met Gln Asn Gln Gly  85                  50                  95 Gly Ala Gly Met Gly Gly Gly Gly Ser Val Asn Ser             100                 105 Ser Leu Gly Gly Asn Ala     110

[0088] This amino acid sequence is encoded by the nucleotide sequence of SEQ. ID. No. 38 as follows: atggactata tcggaaacaa cttttcgaat atcggcaacc tgcagacgat gggcatcggg 60 cctcagcaac acgaggactc cagccagcag tcgccttcgg ctggctccga qcagcagctg 120 gatcagttgc tcgccatgtt catcatgatg atgctgcaac agagccaggg cagcgatgca 180 aatcaggagt gtggcaacga acaaccgcag aacggtcaac aggaaggcct gagtccgttg 240 acgcagatgc tgatgcagat cgtgatgcag ctgatgcaga accagggcgg cgccggcatg 300 ggcggtggcg gttcggtcaa cagcagcctg ggcggcaacg cc 342

[0089] Isolation of Erwinia carotovora hypersensitive response elictor protein or polypeptide is described in Cui et al., “The RsmA Mutants of Erwinia carotovora subsp. carotovora Strain Ecc71 Overexpress hrp N_(Ecc) and Elicit a Hypersensitive Reaction-like Response in Tobacco Leaves,” MPMI, 9(7):565-73 (1996), which is hereby incorporated by reference. This protein has 356 amino acids, a molecular weight of 35.6 kDa, and a pI of 5.82 and is heat stable and glycine rich (21.3%).

[0090] The hypersensitive response elicitor protein or polypeptide of Erwinia stewartii is set forth in Ahmad et al., “Harpin is Not Necessary for the Pathogenicity of Erwinia stewartii on Maize,” 8th Int'l. Cong. Molec. Plant-Microbe Interact., July 14-19, 1996 and Ahmad, et al., “Harpin is Not Necessary for the Pathogenicity of Erwinia stewartii on Maize,” Ann. Mtg. Am. Phytopath. Soc., July 27-31, 1996, which are hereby incorporated by reference.

[0091] Hypersensitive response elicitor proteins or polypeptides from Phytophthora parasitica, Phytophthora cryptogea, Phytophthora cinnamoni, Phytophthora capsici, Phytophthora megasperma, and Phytophora citrophthora are described in Kaman, et al., “Extracellular Protein Elicitors from Phytophthora: Most Specificity and Induction of Resistance to Bacterial and Fungal Phytopathogens,” Molec. Plant-Microbe Interact., 6(1):15-25 (1993), Ricci et al., “Structure and Activity of Proteins from Pathogenic Fungi Phytophthora Eliciting Necrosis and Acquired Resistance in Tobacco,” Eur. J. Biochem., 183:555-63 (1989), Ricci et al., “Differential Production of Parasiticein, and Elicitor of Necrosis and Resistance in Tobacco, by Isolates of Phytophthora parasitica,” Plant Path. 41:298-307 (1992), Baillreul et al, “A New Elicitor of the Hypersensitive Response in Tobacco: A Fungal Glycoprotein Elicits Cell Death, Expression of Defence Genes, Production of Salicylic Acid, and Induction of Systemic Acquired Resistance,” Plant J., 8(4):551-60 (1995), and Bonnet et al., “Acquired Resistance Triggered by Elicitors in Tobacco and Other Plants,” Eur. J. Plant Path., 102:181-92 (1996), which are hereby incorporated by reference. These hypersensitive response elicitors from Phytophthora are called elicitins. All known elicitins have 98 amino acids and show>66% sequence identity. They can be classified into two groups, the basic elicitins and the acidic eliciting, based on the physicochemical properties. This classification also corresponds to differences in the elicitins' ability to elicit HR-like symptoms. Basic elicitins are 100 times more effective than the acidic ones in causing leaf necrosis on tobacco plants.

[0092] The hypersensitive response elicitor from Gram positive bacteria like Clavibacter michiganesis is described in WO 99/11133, which is hereby incorporated by reference.

[0093] The above elicitors are exemplary. Other elicitors can be identified by growing fungi or bacteria that elicit a hypersensitive response using conditions under which genes encoding an elicitor are expressed. Cell-free preparations from culture supernatants can be tested for elicitor activity (i.e. local necrosis) by using them to infiltrate appropriate plant tissues.

[0094] Turning again to the receptor of the present invention for such hypersensitive response elicitors, fragments of the above receptor protein are encompassed by the method of the present invention. In addition, fragments of full length receptor proteins from other plants can also be utilized.

[0095] Suitable fragments can be produced by several means. In the first, subclones of the gene encoding a known receptor protein are produced by conventional molecular genetic manipulation by subcloning gene fragments. The subclones then are expressed in vitro or in vivo in bacterial cells to yield a smaller protein or peptide that can be tested for receptor activity according to the procedure described above.

[0096] As an alternative, fragments of a receptor protein can be produced by digestion of a fall-length receptor protein with proteolytic enzymes like chymotrypsin or Staphylococcus proteinase A, or trypsin. Different proteolytic enzymes are likely to cleave receptor proteins at different sites based on the amino acid sequence of the receptor protein. Some of the fragments that result from proteolysis may be active receptors.

[0097] In another approach, based on knowledge of the primary structure of the receptor protein, fragments of the receptor protein gene may be synthesized by using the PCR technique together with specific sets of primers chosen to represent particular portions of the protein. These then would be cloned into an appropriate vector for expression of a truncated peptide or protein.

[0098] Chemical synthesis can also be used to make suitable fragments. Such a synthesis is carried out using known amino acid sequences for the receptor being produced. Alternatively, subjecting a full length receptor to high temperatures and pressures will produce fragments. These fragments can then be separated by conventional procedures (e.g., chromatography, SDS-PAGE).

[0099] Variants may be made, for example, by altering the gene by the addition of bases encoding amino acids that have minimal influence on the properties, secondary structure, and hydropathic nature of the encoded polypeptide. For example, a polypeptide may be produced that has a signal (or leader) sequence at the N-terminal end of the protein product that co-translationally or post-translationally directs transfer of the protein. The polypeptide, via gene alteration, may also be conjugated to a short 6-10 residue tag or other sequence for ease of synthesis, purification, or identification of the polypeptide

[0100] Suitable DNA molecules are those that hybridize to a DNA molecule comprising a nucleotide sequence of 50 continuous bases of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions characterized by hybridization in buffer comprising 0.9M sodium citrate (“SSC”) buffer at a temperature of 37° C. and remaining bound when subject to washing with the SSC buffer at 37° C.; and preferably in a hybridization buffer comprising 20% formamide in 0.9M saline/0.09M SSC buffer at a temperature of 42° C. and remaining bound when subject to washing at 42° C. with 0.2×SSC buffer at 42° C.

[0101] The receptor of the present invention is preferably produced in purified form (preferably at least about 60%, more preferably 80%, pure) by conventional techniques. Typically, the receptor of the present invention is produced but not secreted into the growth medium of recombinant host cells. Alternatively, the receptor protein of the present invention is secreted into growth medium. In the case of unsecreted protein, to isolate the receptor protein, the host cell (e.g., E. coli) carrying a recombinant plasmid is propagated, lysed by sonication, or chemical treatment, and the homogenate is centrifuged to remove bacterial debris. The cell lysate can be further purified by conventionally utilized chromatography procedures (e.g., gel filtration in an appropriately sized dextran or polyacrylamide column to separate the receptor protein). If necessary, the protein fraction may be further purified by ion exchange or HPLC.

[0102] The DNA molecule encoding the receptor protein can be incorporated in cells using conventional recombinant DNA technology. Generally, this involves inserting the DNA molecule into an expression system to which the DNA molecule is heterologous (i.e. not normally present). The heterologous DNA molecule is inserted into the expression system or vector in sense orientation and correct reading frame. The vector contains the necessary elements for the transcription and translation of the inserted protein-coding sequences.

[0103] U.S. Pat. No. 4,237,224 to Cohen and Boyer, which is hereby incorporated by reference, describes the production of expression systems in the form of recombinant plasmids using restriction enzyme cleavage and ligation with DNA ligase. These recombinant plasmids are then introduced by means of transformation and replicated in unicellular cultures including procaryotic organisms and eucaryotic cells grown in tissue culture.

[0104] Recombinant genes may also be introduced into viruses, such as vaccina virus. Recombinant viruses can be generated in virus infected cells transformed with plasmids.

[0105] Suitable vectors include, but are not limited to, the following viral vectors such as lambda vector system gt11, gt WES.tB, Charon 4, and plasmid vectors such as pBR322, pBR325, pACYC177, pACYC1084, pUC8, pUC9, pUC18, pUC19, pLG339, pR290, pKC37, pKC101, SV 40, pBluescript II SK +/− or KS +/− (see “Stratagene Cloning Systems” Catalog (1993) from Stratagene, La Jolla, Calif., which is hereby incorporated by reference), pQE, pIH821, pGEX, pET series (see F. W. Studier et. al., “Use of T7 RNA Polymerase to Direct Expression of Cloned Genes,” Gene Expression Technology vol. 185 (1990), which is hereby incorporated by reference), and any derivatives thereof Recombinant molecules can be introduced into cells via transformation, transduction, conjugation, mobilization, or electroporation. The DNA sequences are cloned into the vector using standard cloning procedures in the art, as described by Sambrook et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., third edition (2001), which is hereby incorporated by reference.

[0106] A variety of host-vector systems may be utilized to express the protein-encoding sequence(s). Primarily, the vector system must be compatible with the host cell used. Host-vector systems include but are not limited to the following: bacteria transformed with bacteriophage DNA, plasmid DNA, or cosmid DNA; microorganisms such as yeast containing yeast vectors; mammalian cell systems infected with virus (e.g., vaccinia virus, adenovirus, etc.); insect cell systems infected with virus (e.g., baculovirus); and plant cells infected by bacteria. The expression elements of these vectors vary in their strength and specificities. Depending upon the host-vector system utilized, any one of a number of suitable transcription and translation elements can be used.

[0107] Different genetic signals and processing events control many levels of gene expression (e.g., DNA transcription and messenger RNA (mRNA) translation).

[0108] Transcription of DNA is dependent upon the presence of a promotor which is a DNA sequence that directs the binding of RNA polymerase and thereby promotes mRNA synthesis. The DNA sequences of eucaryotic promoters differ from those of procaryotic promoters. Furthermore, eucaryotic promoters and accompanying genetic signals may not be recognized in or may not function in a procaryotic system, and, further, procaryotic promotors are not recognized and do not function in eucaryotic cells.

[0109] Similarly, translation of mRNA in procaryotes depends upon the presence of the proper procaryotic signals which differ from those of eucaryotes. Efficient translation of mRNA in procaryotes requires a ribosome binding site called the Shine-Dalgarno (“SD”) sequence on the mRNA. This sequence is a short nucleotide sequence of mRNA that is located before the start codon, usually AUG, which encodes the amino-terminal methionine of the protein. The SD sequences are complementary to the 3′-end of the 16S rRNA (ribosomal RNA) and probably promote binding of mRNA to ribosomes by duplexing with the rRNA to allow correct positioning of the ribosome. For a review on maximizing gene expression, see Roberts and Lauer, Methods in Enzymology, 68:473 (1979), which is hereby incorporated by reference.

[0110] Promotors vary in their “strength” (i.e. their ability to promote transcription). For the purposes of expressing a cloned gene, it is desirable to use strong promoters in order to obtain a high level of transcription and, hence, expression of the gene. Depending upon the host cell system utilized, any one of a number of suitable promoters may be used. For instance, when cloning in E. coli, its bacteriophages, or plasmids, promoters such as the T7 phage promoter, lac promotor, trp promotor, recA promotor, ribosomal RNA promotor, the P_(R) and P_(L) promoters of coliphage lambda and others, including but not limited, to lacUV5, ompF, bla, lpp, and the like, may be used to direct high levels of transcription of adjacent DNA segments. Additionally, a hybrid trp-lacUV5 (tac) promotor or other E. coli promoters produced by recombinant DNA or other synthetic DNA techniques may be used to provide for transcription of the inserted gene.

[0111] Bacterial host cell strains and expression vectors may be chosen which inhibit the action of the promotor unless specifically induced. In certain operations, the addition of specific inducers is necessary for efficient transcription of the inserted DNA. For example, the lac operon is induced by the addition of lactose or IPTG (isopropylthio-beta-D-galactoside). A variety of other operons, such as trp, pro, etc., are under different controls.

[0112] Specific initiation signals are also required for efficient gene transcription and translation in procaryotic cells. These transcription and translation initiation signals may vary in “strength” as measured by the quantity of gene specific messenger RNA and protein synthesized, respectively. The DNA expression vector, which contains a promotor, may also contain any combination of various “strong” transcription and/or translation initiation signals. For instance, efficient translation in E. coli requires an SD sequence about 7-9 bases 5′ to the initiation codon (“ATG”) to provide a ribosome binding site. Thus, any SD-ATG combination that can be utilized by host cell ribosomes may be employed. Such combinations include but are not limited to the SD-ATG combination from the cro gene or the N gene of coliphage lambda, or from the E. coli tryptophan E, D, C, B or A genes. Additionally, any SD-ATG combination produced by recombinant DNA or other techniques involving incorporation of synthetic nucleotides may be used.

[0113] Once the isolated DNA molecule encoding the receptor protein has been cloned into an expression system, it is ready to be incorporated into a host cell. Such incorporation can be carried out by the various forms of transformation noted above, depending upon the vector/host cell system. Suitable host cells include, but are not limited to, bacteria, virus, yeast, mammalian cells, insect, plant, and the like.

[0114] One aspect of the present invention involves enhancing a plant's receptivity to treatment with a hypersensitive response elicitor by providing a transgenic plant or transgenic plant seed, transformed with a nucleic acid molecule encoding a receptor protein for a hypersensitive response elicitor. It has been found that hypersensitive response elicitors are useful in imparting disease resistance to plants, enhancing plant growth, effecting insect control and/or imparting stress resistance in a variety of plants. In view of the receptor of the present invention's interaction with such elicitors, it is expected that these beneficial effects would be enhanced by carrying out such elicitor treatments with plants transformed with the receptor encoding gene of the present invention.

[0115] Transgenic plants containing a gene encoding a receptor in accordance with the present invention can be prepared according to techniques well known in the art.

[0116] A vector containing the receptor encoding gene described above can be microinjected directly into plant cells by use of micropipettes to transfer mechanically the recombinant DNA. Crossway, Mol. Gen. Genetics, 202:179-85 (1985), which is hereby incorporated by reference. The genetic material may also be transferred into the plant cell using polyethylene glycol. Krens, et al., Nature, 296:72-74 (1982), which is hereby incorporated by reference.

[0117] Another approach to transforming plant cells with a gene is particle bombardment (also known as biolistic transformation) of the host cell. This can be accomplished in one of several ways. The first involves propelling inert or biologically active particles at cells. This technique is disclosed in U.S. Pat. Nos. 4,945,050, 5,036,006, and 5,100,792, all to Sanford et al., which are hereby incorporated by reference, Generally, this procedure involves propelling inert or biologically active particles at the cells under conditions effective to penetrate the outer surface of the cell and to be incorporated within the interior thereof When inert particles are utilized, the vector can be introduced into the cell by coating the particles with the vector containing the heterologous DNA. Alternatively, the target cell can be surrounded by the vector so that the vector is carried into the cell by the wake of the particle. Biologically active particles (e.g., dried bacterial cells containing the vector and heterologous DNA) can also be propelled into plant cells.

[0118] Yet another method of introduction is fusion of protoplasts with other entities, either minicells, cells, lysosomes, or other fusible lipid-surfaced bodies. Fraley, et al.,Proc. Natl. Acad. Sci. USA, 79:1859-63 (1982), which is hereby incorporated by reference.

[0119] The DNA molecule may also be introduced into the plant cells by electroporation. Fromm et al., Proc. Natl. Acad. Sci. USA, 82:5824 (1985), which is hereby incorporated by reference. In this technique, plant protoplasts are electroporated in the presence of plasmids containing the expression cassette. Electrical impulses of high field strength reversibly permeabilize biomembranes allowing the introduction of the plasmids. Electroporated plant protoplasts reform the cell wall, divide, and regenerate.

[0120] Another method of introducing the DNA molecule into plant cells is to infect a plant cell with Agrobacterium tumefaciens or A. rhizogenes previously transformed with the gene. Under appropriate conditions known in the art, the transformed plant cells are grown to form shoots or roots, and develop further into plants. Generally, this procedure involves inoculating the plant tissue with a suspension of bacteria and incubating the tissue for 48 to 72 hours on regeneration medium without antibiotics at 25-28° C.

[0121] Agrobacterium is a representative genus of the gram-negative family Rhizobiaceae. Its species are responsible for crown gall (A. tumefaciens) and hairy root disease (A. rhizogenes). The plant cells in crown gall tumors and hairy roots are induced to produce amino acid derivatives known as opines, which are catabolized only by the bacteria. The bacterial genes responsible for expression of opines are a convenient source of control elements for chimeric expression cassettes. In addition, assaying for the presence of opines can be used to identify transformed tissue.

[0122] Heterologous genetic sequences can be introduced into appropriate plant cells, by means of the Ti plasmid of A. tumefaciens or the Ri plasmid of A. rhizogenes. The Ti or Ri plasmid is transmitted to plant cells on infection by Agrobacterium and is stably integrated into the plant genome. J. Schell, Science, 237:1176-83 (1987), which is hereby incorporated by reference.

[0123] After transformation, the transformed plant cells must be regenerated.

[0124] Plant regeneration from cultured protoplasts is described in Evans et al., Handbook of Plant Cell Cultures, Vol. 1: (MacMillan Publishing Co., New York, 1983); and Vasil I.R. (ed.), Cell Culture and Somatic Cell Genetics of Plants, Acad. Press, Orlando, Vol. 1, 1984, and Vol. III (1986), which are hereby incorporated by reference.

[0125] It is known that practically all plants can be regenerated from cultured cells or tissues, including but not limited to, all major species of sugarcane, sugar beets, cotton, fruit trees, and legumes.

[0126] Means for regeneration vary from species to species of plants, but generally a suspension of transformed protoplasts or a petri plate containing transformed explants is first provided. Callus tissue is formed and shoots may be induced from callus and subsequently rooted. Alternatively, embryo formation can be induced in the callus tissue. These embryos germinate as natural embryos to form plants. The culture media will generally contain various amino acids and hormones, such as auxin and cytokinins. It is also advantageous to add glutamic acid and proline to the medium, especially for such species as corn and alfalfa. Efficient regeneration will depend on the medium, on the genotype, and on the history of the culture. If these three variables are controlled, then regeneration is usually reproducible and repeatable.

[0127] After the expression cassette is stably incorporated in transgenic plants, it can be transferred to other plants by sexual crossing. Any of a number of standard breeding techniques can be used, depending upon the species to be crossed.

[0128] Once transgenic plants of this type are produced, the plants themselves can be cultivated in accordance with conventional procedures. Alternatively, transgenic seeds or propagules (e.g., cuttings) are recovered from the transgenic plants. The seeds can then be planted in the soil and cultivated using conventional procedures to produce transgenic plants. The transgenic plants are propagated from the planted transgenic seeds.

[0129] These elicitor treatment methods can involve applying the hypersensitive response elicitor polypeptide or protein in a non-infectious form to all or part of a plant or a plant seed transformed with a receptor gene in accordance with the present invention under conditions effective for the elicitor to impart disease resistance, enhance growth, control insects, and/or to impart stress resistance. Alternatively, the hypersensitive response elicitor protein or polypeptide can be applied to plants such that seeds recovered from such plants themselves are able to impart disease resistance in plants, to enhance plant growth, to effect insect control, and/or to impart resistance to stress.

[0130] As an alternative to applying a hypersensitive response elicitor polypeptide or protein to plants or plant seeds in order to impart disease resistance in plants, to effect plant growth, to control insects, and/or to impart stress resistance in the plants or plants grown from the seeds, transgenic plants or plant seeds can be utilized. When utilizing transgenic plants, this involves providing a transgenic plant transformed with both a DNA molecule encoding a receptor in accordance with the present invention and with a DNA molecule encoding a hypersensitive response elicitor polypeptide or protein. The plant is grown under conditions effective to permit the DNA molecules to impart disease resistance to plants, to enhance plant growth, to control insects, and/or to impart resistance to stress. Alternatively, a transgenic plant seed transformed with a DNA molecule encoding a hypersensitive response elicitor polypeptide or protein and a DNA molecule encoding a receptor can be provided and planted in soil. A plant is then propagated from the planted seed under conditions effective to permit the DNA molecules to impart disease resistance to plants, to enhance plant growth, to control insects, and/or to impart resistance to stress.

[0131] The embodiment where the hypersensitive response elicitor polypeptide or protein is applied to the plant or plant seed can be carried out in a number of ways, including: 1) application of an isolated elicitor or 2) application of bacteria which do not cause disease and are transformed with a gene encoding the elicitor. In the latter embodiment, the elicitor can be applied to plants or plant seeds by applying bacteria containing the DNA molecule encoding the hypersensitive response elicitor polypeptide or protein. Such bacteria must be capable of secreting or exporting the elicitor so that the elicitor can contact plant or plant seeds cells. In these embodiments, the elicitor is produced by the bacteria in planta or on seeds or just prior to introduction of the bacteria to the plants or plant seeds.

[0132] The hypersensitive response elicitor treatment can be utilized to treat a wide variety of plants or their seeds to impart disease resistance, enhance growth, control insects, and/or impart stress resistance. Suitable plants include dicots and monocots. More particularly, useful crop plants can include: alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, turnip, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane. Examples of suitable ornamental plants are: Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.

[0133] With regard to the use of hypersensitive response elicitors in imparting disease resistance, absolute immunity against infection may not be conferred, but the severity of the disease is reduced and symptom development is delayed. Lesion number, lesion size, and extent of sporulation of fungal pathogens are all decreased. This method of imparting disease resistance has the potential for treating previously untreatable diseases, treating diseases systemically which might not be treated separately due to cost, and avoiding the use of infectious agents or environmentally harmful materials.

[0134] The method of imparting pathogen resistance to plants is useful in imparting resistance to a wide variety of pathogens including viruses, bacteria, and fungi. Resistance, inter alia, to the following viruses can be achieved by the method of the present invention: Tobacco mosaic virus and Tomato mosaic virus. Resistance, inter alia, to the following bacteria can also be imparted to plants Pseudomonas solancearum; Pseudomonas syringae pv. tabaci; and Xanthamonas campestris pv. pelargonii. Plants can be made resistant, inter alia, to the following fungi: Fusarium oxysporum and Phytophthora infestans.

[0135] With regard to the use of the hypersensitive response elicitor protein or polypeptide to enhance plant growth, various forms of plant growth enhancement or promotion can be achieved. This can occur as early as when plant growth begins from seeds or later in the life of a plant. For example, plant growth according to the present invention encompasses greater yield, increased quantity of seeds produced, increased percentage of seeds germinated, increased plant size, greater biomass, more and bigger fruit, earlier fruit coloration, and earlier fruit and plant maturation. As a result, there is significant economic benefit to growers. For example, early germination and early maturation permit crops to be grown in areas where short growing seasons would otherwise preclude their growth in that locale. Increased percentage of seed germination results in improved crop stands and more efficient seed use. Greater yield, increased size, and enhanced biomass production allow greater revenue generation from a given plot of land.

[0136] The use of hypersensitive response elicitors for insect control encompasses preventing insects from contacting plants to which the hypersensitive response elicitor has been applied, preventing direct insect damage to plants by feeding injury, causing insects to depart from such plants, killing insects proximate to such plants, interfering with insect larval feeding on such plants, preventing insects from colonizing host plants, preventing colonizing insects from releasing phytotoxins, etc. The present invention also prevents subsequent disease damage to plants resulting from insect infection.

[0137] Elicitor treatment is effective against a wide variety of insects. European corn borer is a major pest of corn (dent and sweet corn) but also feeds on over 200 plant species including green, wax, and lima beans and edible soybeans, peppers, potato, and tomato plus many weed species. Additional insect larval feeding pests which damage a wide variety of vegetable crops include the following: beet armyworm, cabbage looper, corn ear worm, fall armyworm, diamondback moth, cabbage root maggot, onion maggot, seed corn maggot, pickleworm (melonworm), pepper maggot, tomato pinworm, and maggots. Collectively, this group of insect pests represents the most economically important group of pests for vegetable production worldwide.

[0138] Hypersensitive response elicitor treatment is also useful in imparting resistance to plants against environmental stress. Stress encompasses any environmental factor having an adverse effect on plant physiology and development. Examples of such environmental stress include climate-related stress (e.g., drought, water, frost, cold temperature, high temperature, excessive light, and insufficient light), air pollution stress (e.g., carbon dioxide, carbon monoxide, sulfur dioxide, NO_(x), hydrocarbons, ozone, ultraviolet radiation, acidic rain), chemical (e.g., insecticides, fungicides, herbicides, heavy metals), and nutritional stress (e.g., fertilizer, micronutrients, macronutrients).

[0139] The application of the hypersensitive response elicitor polypeptide or protein can be carried out through a variety of procedures when all or part of the plant is treated, including leaves, stems, roots, etc. This may (but need not) involve infiltration of the hypersensitive response elicitor polypeptide or protein into the plant. Suitable application methods include high or low pressure spraying, injection, and leaf abrasion proximate to when elicitor application takes place. When treating plant seeds or propagules (e.g., cuttings), the hypersensitive response elicitor protein or polypeptide can be applied by low or high pressure spraying, coating, immersion, or injection. Other suitable application procedures can be envisioned by those skilled in the art provided they are able to effect contact of the elicitor with cells of the plant or plant seed. Once treated with a hypersensitive response elicitor, the seeds can be planted in natural or artificial soil and cultivated using conventional procedures to produce plants. After plants have been propagated from seeds treated with an elicitor, the plants may be treated with one or more applications of the hypersensitive response elicitor protein or polypeptide to impart disease resistance to plants, to enhance plant growth, to control insects on the plants, and/or to impart stress resistance.

[0140] The hypersensitive response elicitor polypeptide or protein can be applied to plants or plant seeds alone or in a mixture with other materials. Alternatively, the elicitor can be applied separately to plants with other materials being applied at different times.

[0141] A composition suitable for treating plants or plant seeds contains a hypersensitive response elicitor polypeptide or protein in a carrier. Suitable carriers include water, aqueous solutions, slurries, or dry powders.

[0142] Although not required, this composition may contain additional additives including fertilizer, insecticide, fungicide, nematacide, and mixtures thereof Suitable fertilizers include (NH₄)₂NO₃. An example of a suitable insecticide is Malathion. Useful fungicides include Captan.

[0143] Other suitable additives include buffering agents, wetting agents, coating agents, and abrading agents. In addition, the hypersensitive response elicitor can be applied to plant seeds with other conventional seed formulation and treatment materials, including clays and polysaccharides.

[0144] In the alternative technique involving the use of transgenic plants and transgenic seeds encoding a hypersensitive response elicitor encoding gene, a hypersensitive response elicitor need not be applied topically to the plants or seeds. Instead, transgenic plants transformed with a DNA molecule encoding such an elicitor are produced according to procedures well known in the art as described above.

[0145] In another embodiment, the present invention relates to a DNA construct which is an antisense nucleic acid molecule to a nucleic acid molecule encoding a receptor in plants for plant pathogen hypersensitive response elicitors. An example of such a construct would be an antisense DNA molecule of the DNA molecule having the nucleotide sequence of SEQ. ID. Nos. 2, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, or35 (or a portion thereof). Alternatively, the DNA construct can have a DNA molecule having the nucleotide sequence of SEQ. ID. Nos. 2, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, or 35 (or a portion thereof) and its complementary strand and is used to generate a single transcript with an inverted repeat (i.e. a double-stranded) RNA. This transcript as well as the above-discussed antisense nucleic acid molecule can be used to induce silencing of a nucleic acid molecule encoding a receptor for a hypersensitive response elicitor.

[0146] Sensing the hypersensitive response elicitor by the receptor is the very first step of the signal transduction pathway in plants which eventually leads to disease resistance, growth enhancement, insect control, and stress resistance. Silencing the receptor provides a powerful tool to find and study the downstream components of this pathway. Additionally, the receptor could be a negative regulator of such plant signal transduction pathway. Silencing of the receptor will impart to plants the ability to resist disease and stress, control insects, and enhance growth without hypersensitive response elicitor treatment.

EXAMPLES Example 1 Materials and Methods

[0147] The laboratory techniques used in the following example are routine. All DNA manipulations described here followed conventional protocols (Sambrook et al., “Molecular Cloning: A Laboratory Manual,” 2nd ed., Cold Spring Harbor Laboratory (1989); Ausubel, et al., “Current Protocols in Molecular Biology,” John Wiley (1987), which are hereby incorporated by reference). The plasmids and microorganisms described herein, used for making the present invention, were obtained from commercial sources, or from the authors of previous publications. Sequences were analyzed with Clone Manager 5 (Scientific & Educational Software, Durham, N.C.).

[0148] Yeast strain L40 was grown in YPD or in different minimal synthetic dropout selection media at 30° C. E.coli strains DH5α and HB101 were grown in LB at 37° C.

[0149] The yeast Two-Hybrid system is based on the fact that many eukaryotic transcription factors are composed of a physically separable, functionally independent DNA-binding domain (DNA-BD) and an activation domain (AD). Both the DNA-BD and the AD are required to activate a gene. When physically separated by recombinant DNA technology and expressed in the same host cell, the DNA-BD and the AD do not interact directly with each other and, thus, cannot activate the responsive gene (Ma, et al., “Converting a Eukaryotic Transcriptional Inhibitor into an Activator,” Cell 55:443 (1988) and Brent, et al., “A Eukaryotic Transcriptional Activator Bearing the DNA Specificity of a Prokaryotic Repressor,” Cell 43:729 (1985), which are hereby incorporated by reference). But if the DNA-BD and the AD are brought into close physical proximity in the promoter region, the transcriptional activation function will be restored. Therefore, the yeast Saccharomyces cerevisiae and the Two-Hybrid system have become essential genetic tools for studying the macromolecular interactions.

[0150] In the Two-Hybrid system utilized here, the DNA-BD, encoded in the bait vector pVJL11 (Jullien-Flores, V., “Bridging Ral GTPase to Rho Pathways. RLIP76, a Ra1 Effector with CDC42/Rac GTPase-activating Protein Activity,” J. Biol. Chem. 27:22473 (1995), which is hereby incorporated by reference), is the prokaryotic LexA protein, and the activation domain, encoded in the prey vector pGAD 10 or pGAD GH (Clontech; Hannon, G J., “Isolation of the Rb-related p130 Through its Interaction with CDK2 and Cyclins,” Genes Dev. 7:2378 (1993), which is hereby incorporated by reference) is derived from the yeast GAL4 protein. pVJL11 also has a TRP1 marker, and the pGAD has a LEU2 marker. An interaction between the bait protein (fused to the DNA-BD) and a library-encoded protein (fused to the AD) creates a novel transcriptional activator with binding affinity for LexA operators. The yeast host L40 {MATa his3D200 trp1-901 leu2-3, 112 ade2 LYS2::(lexAop)₄-HIS3 URA3:: (lexAop)₈-lacZ} harbors two reporter genes, lacZ and HIS3, which contain upstream LexA binding site. The HIS3 nutritional reporter provides a sensitive growth selection that can identify a single positive transformant out of several million candidate clones. The expression of the reporter genes indicates interaction between a candidate protein and the bait protein. See FIG. 1.

[0151]Erwinia amylovora harpin was used as the bait protein to screen the Arabidopsis thaliana MATCHMAKER cDNA library cloned in the pGAD 10 vector (Clontech Laboratories, Inc., Palo Alto, Calif.). One cDNA library encoded protein was identified as a strong harpin interacting protein and, thus, a putative harpin receptor. The present invention reports the nucleic acid sequence and the deduced amino acid sequence of this cDNA.

Example 2

[0152] HrpN of Erwinia amylovora was subcloned into the yeast Two-Hybrid bait vector pVJL11. PCR was carried out using the 1.3 kb harpin fragment (Wei et al., “Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora,” Science 257:85 (1992), which is hereby incorporated by reference) as a template to amplify the harpin encoding region. A BamHI site was added to the 5′ end of the coding sequence, and a SalI site to the 3′ end. A BamHI and SalI digested PCR fragment was ligated with the bait vector pVJL11 digested with the same restriction enzymes. pVJL11 has a TRP1 marker for selection in yeast and an Ampicillin resistance marker for selection in E. coli. The plasmid DNA was amplified in E. coli strain DH5α. When tested in the Two-Hybrid system with empty prey vector pGAD GH and several unrelated proteins, HrpN did not show auto-activation or nonspecific interaction with unrelated proteins, as shown in FIG. 2.

Example 3

[0153] HrpN-pVJL 11 was transformed into yeast strain L40 by a lithium acetate (LiAc)-mediated method (Ito et al., “Transformation of Intact Yeast Cells Treated with Alkali Cations,” J. Bacteriol. 153:163 (1983) and Vojtek et al., “Mammalian Ras Interacts Directly with the Serine/Threonine Kinase Raf,” Cell 74:205 (1993), which are hereby incorporated by reference). The Arabidopsis thaliana MATCHMAKER cDNA library (Clontech Laboratories, Inc., Palo Alto, Calif.) was screened for harpin interacting proteins. Approximately 6.8 million primary library transformants were plated onto plates lacking histidine, leucine, and tryptophan. A total of 148 colonies grew on the histidine dropout plates, 55 of which stained positive when tested for expression of β-galactosidase. After three rounds of selection on synthetic minimal (SD) media plates lacking leucine, tryptophan, and histidine, and confirming by the expression of the second reporter gene lacZ using a β-galactosidase assay, 47 colonies seemed to be strong interacting candidates.

Example 4

[0154] Plasmid DNA was extracted from the 47 independent yeast colonies and shuttled into E.coli strain HB101, which carries the leuB mutation. Therefore, the prey plasmid (cDNA-pGAD 10) was selected for on minimal nutrient plates since pGAD 10 bears the LEU2 marker.

[0155] The 47 independently rescued prey plasmids purified from E. coli were retested in the yeast two-hybrid system with harpin as bait. They were also tested against unrelated proteins. 25 turned out to be interacting candidates, 20 of which were strong specific interacting candidates. Sequencing analysis showed that the 20 independent cDNA clones were actually from the same gene with different integrity at their 5′ end. The sequence reactions were performed using the PE Prism BigDye™ dye terminator reaction kit. The sequencing gel was run in Thatagen (Bothell, Wash.).

[0156] One of the eight plasmids, which had the longest cDNA insert of 1 kb, was used for further analysis. When co-transformed into yeast strain L40, it was shown to be negative with empty bait and unrelated proteins in the Two-Hybrid system, indicating the specificity of the interaction between harpin and this receptor candidate. See FIG. 3.

Example 5

[0157] The longest cDNA insert, designated AtHrBP1 (Arabidopsis thaliana harpin-binding-protein 1), was subcloned into the BamHI and SalI sites of the bait vector pVJL11. This construct did not show auto-activation of the reporter genes, nor interaction with unrelated proteins in the yeast Two-Hybrid system. However, the expression of the reporter genes was activated when L40 was co-transformed with AtHrBP1-pVJL11 and hrpN-pGAD GH, indicating the specific interaction between AtHrBP1p (“p” distinguishing the protein encoded byAtHrBP1) and harpin. See FIG. 4.

Example 6

[0158] Total RNA was extracted from two-week-old Arabidopsis thaliana using QIAGEN RNeasy plant mini kit (Qiagen, Inc., Valencia, Calif.). Poly A⁺ RNA was further purified from the total RNA with a QIAGEN Oligotex column (Qiagen, Inc., Valencia, Calif.). A Northern blot was carried out using the translated region of AtHrBP1 as a probe. One single species with an apparent molecular weight of about 1.1 kb was detected from both total RNA and Poly A⁺ RNA. Therefore, the longest cDNA of AtHrBP1 from the yeast two-hybrid screen seems to be the full-length cDNA. The integrity of the 5′ of cDNA was further confirmed by a primer extension assay.

[0159] As described, the yeast Two-Hybrid system was used to screen for harpin interacting proteins. hrpn of Erwinia amylovora was subcloned into the yeast Two-Hybrid bait vector pVJL11, which has a TRP1 marker. The lexA-harpin fusion protein is expressed from this construct in yeast. The Arabidopsis thaliana MATCHMAKER cDNA library (Clontech Laboratories, Inc., Palo Alto, Calif.) was screened for hypersensitive response elicitor interacting proteins. 6.8 million independent colonies were screened, and AtHrBP1 was identified as a strong specific harpin interacting candidate. AtHrBP1 was mapped to Arabidopsis thaliana genomic DNA, chromosome 3, P1 clone MLM24 (Nakamura, “Structural Analysis of Arabidopsis thaliana chromosome 3,” Direct submission to the DDBJ/EMBL/GenBank databases (1998), which is hereby incorporated by reference). Four exons and three introns were discovered (See FIG. 5). Exon 4 includes a 130 bp non-translated 3′ region. The in-frame open reading frame from the first methionine encodes a polypeptide of 284 amino acids, AtHrBP1p. The predicted molecular weight of AtHrBP1p is 30454.3 and the predicted pI is 5.72. There is no apparent hydrophobic trans-membrane domain in this polypeptide. The AtHrBP1-AD fusion prey was negative with empty bait and unrelated proteins in the yeast 2-H system, indicating the specificity of the interaction between harpin and this receptor candidate. When tested in the opposite orientation, i.e. AtHrBP1p fused with the DNA-BD and harpin with the AD, they still specifically interacted with each other.

Example 7

[0160] The AtHrBP1 cDNA was subcloned into the NdeI and SalI sites of the vector pET-28a (Novagen, Madison, Wis.). AtHrBP1p was expressed from this vector in E. coli as a His-tagged protein and purified with Ni-NTA resion (QIAGEN Inc., Valencia, Calif.) according to the manual provided by the manufacturer. This recombinant protein increased harpin's ability to induce HR in tobacco plants. Recombinant AtHrBP1p with the His-tag removed was used to generate anti-AtHrBP1p antibody to facilitate biochemical and functional studies of AtHrBP1p. Preliminary localization studies using anti-AtHrBP1p antibody in a Western blot showed that AtHrBP1p exists everywhere in Arahidopsis, including its leaves, stems, roots, flowers and seeds and that it is most likely cell wall bound.

Example 8

[0161] Ten μg of total RNA from 14 different plant species was separated on a 1% agarose gel, and then transferred to Amersham Hybond NX membrane (Amersham Pharmacia Biotech, Piscataway, N.J.). The RNA probe, which was complementary to bases 651-855 of AtHrBP1 coding region, was generated using Ambion Strip-EZ RNA kit (Ambion Inc., Houston, Tex.). Membrane hybridization was done with Ambion ULTRAhyb (Ambion Inc., Houston, Tex.), procedure according to manufacturer recommendation.

[0162] The sequence of the AtHrBP1 fragment used to generate the Northern probe (SEQ. ID. No. 39) is as follows: gatcaagata acatttgaga aaacaactgt gaagacatcg ggaaacttgt cgcagattcc 60 tccgtttgat atcccgaggc ttcccgacag tttcagacca tcgtcaaacc ctggaactgg 120 ggatttcgaa gttacctatg ttgatgatac catgcgcata actcgcgggg acagaggtga 180 acttagggta ttcgtcattg cttaa 205

[0163] This Northern blot picked up a band with similar size as AtHrBP1 in all the plant species tested, including tobacco, wheat, corn, citrus, cotton, grass, pansy, pepper, potato, tomato, soybean, sun flower, and lima bean. This indicated that HrBP1-like genes exist universally. See FIG. 6.

Example 9

[0164] An HrBP1 homologue from rice, R6, was cloned by the yeast two-hybrid screening method, using harpin as bait. It not only interacted with fall length harpin but also interacted with a harpin fragment that contains the second HR domain (see FIG. 7). However, it was not a full-length cDNA; there was 5′ end sequence information missing. The R6 partial sequence from rice encoded a peptide of 203 amino acids (R6p). The predicted amino acid sequences for R6p and for AtHrBP1p were compared. Their similarity extended from amino acid 84 through amino acid 284 of AtHrBP1p. The proteins were 74.4% identical and 87.2% similar at the predicted amino acid level, and the two genes were 65% identical at the DNA level.

Example 10

[0165] To obtain a full length rice-HrBP1 homologue, cDNA was prepared from total rice RNA using the R6-specific antisense primer R6NL2 (based on the partial sequence obtained from the yeast two-hybrid screening) (see Table 1) and the 5′ RACE System kit purchased from GIBCO-BRL Life Technologies. The cDNA was then dC-tailed and amplified by the polymerase chain reaction (PCR). The PCR reaction utilized the Advantage-GC2 polymerase mix (Clontech), R6NL1B (see Table 1) as the 3′ primer, and either a polyG-containing primer (Abridged Anchor Primer, Gibco-BRL) or R6NL6 (see Table 1) as the 5′ primer. PCR with the generic primer was performed first. Based on the sequencing results from clones obtained, R6NL6 was designed and used for a second cloning strategy, which started from a fresh batch of RNA (same tissue) and yielded a new batch of clones. The PCR products were gel-purified, cloned into pT-Adv (Clontech), and screened by restriction enzyme digestions prior to sequencing on both strands. Sequencing primers used were: the T7 promoter primer, the M13 reverse primer, R6NL1B, or R6NL4 (see Table 1).

[0166] 3′ RACE was conducted using a kit and reagents from Ambiol (First Choice RLM RACE Kit), which included a polyT primer. The 3′ portion of the R6 gene was amplified by PCR using the R6-specific primer R6NL11 (designed from the partial sequence obtained from the yeast Two-hybrid screening) (see Table 1), a 3′ RACE primer supplied with the kit called 3′ RACE OUTER, and Advantage-GC2 polymerase mix (Clontech). A second round of PCR was done with the R6-specific primer R6NL10 (see Table 1), a 3′ RACE primer supplied with the kit called 3′ RACE INNER, and Advantage-GC2 polymerase mix. The PCR products were cloned into vector pBluescript SK- and sequenced using the T7 promoter primer and the T3 promoter primer. TABLE 1 Gene-specific primers used in 5′ and 3′ RACE. 5′ RACE outer primer 5′ RACE inner primer 3′ RACE outer primer 3′ RACE inner primer PB7 PB9 PB8 bar- ACGAGAAGGCGTTGCTGTAGACCA AGCTTGATTTTCAGCGAGGGGATG ACCTCAACCTCCACCCATTCTC n/a ley (SEQ. ID. No. 40) (SEQ. ID. No. 41) (SEQ. ID. No. 42) PB16 PB3 mai- CTTCTCGAACGTGATCTTGATGC ATGTTGTCGAAGTCGCGGCTCACCA n/a n/a ze (SEQ. ID. No. 43) (SEQ. ID. No. 44) PB 13 PB14 PB15 PB17 po- TAGCTCCTTGGCAGCCTCAT GTGACTTCATCAATACCCGACTG GCTCAACCATGGCTTCTCTACTTC CACTTTTATTGAGCCACCTGGTAG tato (SEQ. ID. No. 45) (SEQ. ID. No. 46) (SEQ. ID. No. 47) (SEQ. ID. No. 48) PB 10 PB 11 PB15 to- CTGACCAAGAGTGATGGGAAGAAG CAAGAGTACGAGATGAGAATGCAC (as above) n/a mato (SEQ. ID. No. 49) (SEQ. ID. No. 50) PB19 PB2O PB21 PB22 wh- ACGAGAAGGCGCTGCTGTAGAC GCGCTCAGCAGCTTGATTTTC TTGCTCTCCTCGATCGATTGAC ATCGCCGTCGTGGTCATCTTGC eat (SEQ. ID. No. 51) (SEQ. ID. No. 52) (SEQ. ID. No. 53) (SEQ. ID. No. 54)

[0167] DNA sequences from several clones were aligned using the Clone Manager 5/SE Central suite of programs. Clones fell into 1 of 2 groups that differed in sequence at discrete locations 5′, 3′, and within the R6 sequence. Clones resembling the original R6 sequence obtained from yeast Two-hybrid screening were designated OsHrBP1-1 and the other clones were called OsHrBP1-2. All clones belonged to either the OsHrBP1-1 group or the OsHrBP1-2 group.

Example 11

[0168] The GenBank dBEST and non-redundant databases were searched for HrBP1 gene family members using the AtHrBP1p amino acid sequence and the search program TBLASTN with default parameters (Altschul et al., “Gapped BLAST and PS 1-BLAST: A New Generation of Protein Database Search Programs,” Nucl. Acids Res. 25:3389-402 (1997), which is hereby incorporated by reference). Partial HrBP1 cDNA sequences were identified from the following crop plants: barley, maize, potato, soybean, tomato, and wheat.

[0169] Appropriate primers were then designed for the above crops, with the exception of soybean, to perform rapid amplification of cDNA ends (RACE) using the FirstChoice RLM-RACE kit (Ambion) according to the manufacturer's instructions. This strategy employs, in the first rounds of amplification, an initial gene-specific primer (outer primer) in combination with an adapter-specific primer, followed by a second round of amplification using another adapter-specific primer and another gene-specific primer (inner primer), which hybridizes downstream of the outer primer region and does not overlap with it. For 3′ RACE a second round of amplification with an inner primer is sometimes not necessary. Table 1 shows sequences of gene-specific primers used in 5′ and 3′ RACE reactions with cDNA samples from the above crop plants. Primers were synthesized by Integrated DNA Technologies, Inc (Coralville, Iowa).

[0170] In the case of wheat and grape, the primers listed in Table 1 yielded two different, but highly conserved HrBP 1 sequences. Confirmation that the resulting 5′ and 3′ RACE products belonged to the same cDNA was performed by either confirming the identity of overlapping sequences in 5′ and 3′ products, or by isolating full-length cDNAs using 3′ RACE gene-specific primers designed to hybridize in the 5′ untranslated region (UTR). TABLE 2 Degenerate primers used in 5′ and 3′ RACE. Primer sequence corresponding to amino acid sequence 5′ RACE outer primer PB27 TCRAAYTTRTGNGCNARNGTNGC ATLAHKFE (SEQ. ID. No. 61) (SEQ. ID. No. 62) 5′ RACE inner primer PB1 ATICKYTGRAAIACYTG QVFQRI (SEQ. ID. No. 63) (SEQ. ID. No. 64) G3′ RACE outer primer PB24 TNWSNGGNYTNAAYMGNGGNYT VSGLNRGL (SEQ. ID. No. 65) (SEQ. ID. No. 66) G3′ RACE inner primer PB26 GNCARGTNTTYCARMGNATHGA GQVFQRID (SEQ. ID. No. 67) (SEQ. ID. No. 68)

[0171] With respect to the soybean GmHrBP1 sequence, after a partial sequence had been identified from dBEST and non-redundant databases searches, clones were purchased from InCyte Genomics and sequenced. A fill length GmHrBP1 sequence was obtained using standard, vector specific sequencing primers.

[0172] Comparison of the deduced amino acid sequences of HrBP1 cDNAs thus far obtained, lead to the identification of regions of conserved motifs (further described in Example 12). From these regions, degenerate primers were designed in order to amplify HrBP1-like cDNAs from plants for which no HrBP1 sequences were available. Table 2 shows sequences of successfully used degenerate primers. Degenerate primers were used to amplify 5′ and 3′ RACE products from plant cDNA preparations. Subsequently, specific primers designed to hybridize in the 5′ and 3′ UTR regions were employed to amplify cDNA fragments with a full-length open reading frame. In this manner, HrBP1 sequence information was obtained from species of grapefruit, cotton, apple, tobacco, and grape.

[0173] Table 3 summarizes the receptors for hypersensitive response elicitors identified and isolated from crop plant by the methods described above. TABLE 3 nucleo- Original tides in amino Molecu- Genbank longest acids lar mass accession Gene name Plant cDNA encoded pI (kDa) number CpHrBP1 grapefruit 1103 285 9.61 31.3 none GhHrBP1 cotton 1064 277 9.37 30.0 none GmHrBP1 soybean 1075 265 7.88 28.4 BG043054 HvHrBP1 barley 1129 277 9.35 29.3 BE216663 LeHrBP1 tomato 1026 276 6.25 30.1 AI779661 MdHrBP1 apple 1138 282 8.96 30.2 none NtHrBP1 tobacco 1044 276 8.80 30.0 none OsHrBP1-1 rice 1123 270 8.92 28.4 none OsHrBP1-2 rice 1112 269 8.56 28.2 none StHrBP1 potato 1078 275 8.31 30.1 BE923126 TaHrBP1-l wheat 1057 277 9.64 29.4 BG907618 TaHrBP1-2 wheat 1205 275 7.75 30.0 BG908482 VsHrBP1-1 grape 1038 291 7.82 31.4 none VsHrBP1-2 grape 1055 292 7.82 31.5 none ZmHrBP1 maize 1218 272 9.57 29.3 BG319894

Example 12

[0174] The HrBP1 amino acid and nucleotide sequences were analyzed and compared using several different techniques. The cDNA open reading frame or amino acid sequences were compared using the program Align Plus 4. DNA comparisons used a standard linear scoring matrix; amino acid comparisons used the BLOSUM 62 scoring matrix (See Tables 4). FIG. 8 shows a comprehensive comparison of the HrBP1p amino acid sequences constructed with the use of the GeneDoc program (Nicholas, K. B., Nicholas H. B. Jr., and Deerfield, D. W. II. 1997 GeneDoc: Analysis and Visualization of Genetic Variation, EMBNEW.NEWS 4:14, which is hereby incorporated by reference). TABLE 4 Percent identity of predicted open reading frame and amino acid sequences of HrBP1 cDNAs. Figures in white boxes represent DNA sequence identity; figures in shaded boxes represent amino acid sequence identity.

Example 14

[0175] Based on the HrBP1p amino acid comparisons described in Example 13, regions of highly conserved amino acid sequences were identified. Identification of these regions further enabled identification of specific motifs throughout the conserved region of HrBP1p. As a result of this analysis, several blocks of 5 or more identical amino acids were found as shown in Table 5. TABLE 5 Location in AtHrBP1p (SEQ. ID. No. 1) Motif  97-102 GLNRGL (SEQ. ID. No. 69) 143-148 YSSAFS (SEQ. ID. No. 70) 168-177 TLGQVFQRID (SEQ. ID. No. 71) 182-186 DFDNI (SEQ. ID. No. 72) 203-211 TATLAHKFE (SEQ. ID. No. 73) 271-275 TRGDR (SEQ. ID. No. 74) 277-282 ELRVFV (SEQ. ID. No. 75)

[0176] In addition, several blocks of 5 or more conserved amino acids were found as shown in Table 6. TABLE 6 Location in AtHrBP1p Motif  97-102 GLNRGL (SEQ. ID. No. 69) 115-120 AA42LE (SEQ. ID. No. 76) 135-148 LQG4W4L6YSSAFS (SEQ. ID. No. 77) 150-154 R3LGG (SEQ. ID. No. 78) 162-178 GRL6P6TLGQVFQRID6 (SEQ. ID. No. 79) 182-186 DEDNI (SEQ. ID. No. 72) 203-212 TATLAHKFE6 (SEQ. ID. No. 80) 225-229 T3VKT (SEQ. ID. No. 81) 261-265 VT56D (SEQ. ID. No. 82) 269-275 R6TRGDR (SEQ. ID. No. 83) 277-283 ELRVFV6 (SEQ. ID. No. 84)

[0177] The information presented in Table 5 can be combined to define the receptor of the present invention as having an amino acid sequence of SEQ. ID. No. 85 (with X being any amino acid) as follows:

[0178] (79-104X)GLNRGL(40-42X)YSSAFS(19X)TLGQVFQRID(4X)DFDNI(16X) TATLAHKFE(59-60X)TRGDR(X)ELRVFVXX

[0179] The information from Table 6 can be combined to define the receptor of the present invention as having an amino acid sequence of SEQ. ID. No. 86 as follows (with X being any amino acid and 2, 3, 4, 5, and 6 having the same definitions as for Table 6):

[0180] (79-104X)GLNRGL(12X)AA42LE(14-16X)LQG4W4L6YSSAFS(X)R3LGG(7X) GRL6P6TLGQVFQRID6(3X)DFDNI(16X)TATLAHKFE6(12X)T3VKT(31-32X)VT56D(3X)R6TRGDRXELRVFV6X

Example 14

[0181] In order to further evaluate the highly conserved C-terminal region of the HrBP1p proteins and its potential role in the observed interaction between HrBP1p and harpin, AtHrBP1 deletion mutants were constructed and used in conjunction with hrpN in additional yeast-two hybrid studies. Six AtHrBP1 deletion mutants were analyzed with respect to their ability to interact with full-length harpin. The deletion mutants were cloned into the bait vector pVJL 11. Yeast strain L40 cells were then co-transformed with the AtHrBP1 deletion mutant bait constructs, and haprin cloned in the prey vector pGAD GH. The yeast-two hybrid assays were conducted including the proper controls as described above. FIG. 9 details the exact AtHrBP1p fragments analyzed, as well as the the outcome of the assays. Interaction between harpin and AtHrBP1p deletion mutant proteins was only observed with mutants containing amino acids 80-284 and 84-284. The results indicated that substantially the entire conserved region, as described earlier in Examples 13 and 14, is required for interaction between harpin and AtHrBP1p.

Example 15

[0182] Affinity chromatography is a powerful method for characterizing and isolating components of protein complexes (Formosa et al., “Using Protein Affinity Chromatography to Probe Structure of Protein Machines”, Methods in Enzymol. 208:24-45 (1991), which is hereby incorporated by reference). Affinity chromatography was used to verify that the binding observed between AtHrBP1p and HrpN in the yeast two-hybrid assay was specific and independent of the other protein components of that assay (LexA BD, GAL4 AD). Highly purified HrpN was prepared and conjugated to agarose beads, which were then incubated with partially purified AtHrBP1p (FIG. 10, lanes 2 and 3, respectively). The unbound proteins were collected and the beads were washed extensively with binding buffer, followed by buffers with increasing concentrations of NaCl. The proteins in the fractions were separated by SDS-PAGE and visualized by silver staining. A comparison of the proteins in the load and unbound proteins in the flow-through fractions showed that nearly all the AtHrBP1p in the load was retained on the HrpN matrix (HrpN), whereas no significant binding to the mock-conjugated matrix (C) was observed (FIG. 11A). The efficiency of binding of AtHrBP1p to the HrpN matrix (>95%) and to the control matrix (<5%) was determined in replicate experiments (n =4, not shown). Very little or no AtHrBP1p eluted from the HrpN matrix when high salt buffers were applied (FIG. 11A). This suggested that the binding between HrpN and AtHrBP1p was very tight.

[0183] The experiment was repeated with CHAPS detergent (0.2% w/v) included in the binding, wash, and elution buffers. In this case, AtHrBP1p was eluted in a very pure state from the HrpN matrix using moderately high salt (FIG. 11B). Elution required at least 200 mM NaCl and was more efficient with 500-1500 mM NaCl. This result demonstrates that HrBP1p binds specifically to HrpN.

[0184] When CHAPS was included in the binding buffer, the total amount of AtHrBP1p bound to the HrpN matrix (˜75-70% bound, replicates not shown) was reduced. The CHAPS probably prevented non-specific interactions between proteins and the beads, as shown by the following observations. The inclusion of CHAPS in buffers stripped some of the HrpN from beads, causing it to appear in the flow-through. This probably accounted for some of the reduced binding by AtHrBP1p to the matrix. This effect by detergent on HrpN suggests that some HrpN was adsorbed nonspecifically to to the matrix rather than cross-linked to it. It was also observed that high salt buffers containing CHAPS eluted the tightly held AtHrBP1p that was bound to HrpN matrix in the absence of the detergent; some HrpN and small amounts of other proteins eluted with it. Trace amounts of AtHrBP1p (<5% of the load) and small amounts of other proteins also eluted from mock-conjugated beads treated this way. Therefore, the CHAPS improved the specificity of the AtHrBP 1p-HrpN interaction by decreasing interactions between proteins and the agarose beads.

[0185] AtHrBP1p has a large trypsin-resistant fragment, designated TL-HrBP1p (-25 kDa; FIG. 10, lane 4) that initiates with residue 52 of the full-length AtHrBP1p. TL-HrBP1p could also be missing residues from the C-terminus of the protein since there are 4 potential cleavage sites within the last 16 amino acids at the end. Purified TL-HrBP1p was tested for its ability to bind to HrpN matrix in the presence of CHAPS. A significant percentage (40%) of the input TL-HrBP1p was specifically retained on the HrpN matrix. This result confirms the observation made using the yeast two-hybrid assay that the C-terminal conserved region of the protein is largely responsible for its interaction with HrpN. Residues missing from TL-HrBP1p as a result of the proteolysis might normally contribute to the strength of the interaction between AtHrBP1p and HrpN.

Example 16

[0186] A transgenic approach was used for functional analysis of AtHrBP1p. Anti-sense AtHrBP1, which is complementary to SEQ. ID. No. 2, was sub-cloned into binary vector pPZP212, and is under the control of the NOS promoter. Arabidopsis thaliana plants were transformed with this construct via an Agrobacteria mediated method. The Agrobacterium tumefaciens strain used was GV3101 (C58C1 Rifr) pMP90 (Gmr). These antisense lines were designated “as” lines.

[0187] Arabidopsis plants were also transformed with a construct, which has an inverted repeat with a sense strand of AtHrBP1 coding region bases 4-650 (i.e. bases 20-666 of SEC. ID. No. 2) and the complementary sequence of bases 20-516 of AtHrBP1 cDNA (i.e. SEQ. ID. No. 2). This construct generated a double-stranded mRNA in transformed plants. These transgenic lines were designated “d” lines.

[0188]FIG. 12 shows the constructs used to transform Arabidopsis.

[0189] Both antisense and double-stranded approaches were to silence the expression of AtHrBP1. The double stranded RNA method was found to be more efficient in silencing the AtHrBP1 gene. Some transgenic Arabidopsis lines showed spontaneous HR-mimic lesion. The most severe line was developmentally retarded, looked very unhealthy, and did not produce seeds. The transgenic and control Arabidopsis thaliana Columbia plants were grown in autoclaved potting mix in a controlled environment room at a day and night temperature of 23-20° C. and a photoperiod of 14 h light.

Example 17

[0190] Plants were grown in autoclaved potting mix in a controlled environment room with a day and night temperature of 23-20° C. and a photoperiod of 14 h light. 25-day-old plants were inoculated with Pseudomonas syringae p.v. tomato DC3000 by dipping the above soil parts of the plants in 10⁸ cells ml⁻¹ bacteria suspension for 10 second. Seven days after DC3000 inoculation, leaf disks were harvested with a cork borer. Bacteria were extracted from leaf disks in 10 mM MgCl₂ and plated on King's B agar containing 100 μg rifampicin/ml. Plates were incubated at 28° C. for 2 days (FIG. 13B) and colonies were counted. In FIG. 13A, wild type Arabidopsis plants had significantly more disease development than transgenic plants. Bacteria counting (FIG. 13C) showed that transgenic plants had at least one order of magnitude less of DC3000 growing inside the leaves. AtHrBP1p appeared to function like a negative regulator of plant defense signal transduction pathway in Arabidopsis. Its silencing imparted plants with the ability to resist Pseudomonas syringae p.v. tomato DC3000.

Example 18

[0191] Wild type Col-0 Arabidopsis plants and three independent AtHrBP1 suppression lines were grown in soil mix 1:1:1 (Sunshine LC1: perlite: coarse vermiculite) in a controlled environment room with a day and night temperature of 23-20° C. and photoperiod of 16 hour light. The suppression lines progressed to different growth/developmental stages faster than wild type plants. In comparing plants at the same growth stage, the suppression lines were larger than wild type plants. FIG. 14A shows data evaluating the percentage of plants with 4 true leaves>1 mm in length at sequential days after sowing. As shown, most suppression lines grew to this stage 2 days earlier than wild type plants. FIG. 14B details data regarding the diameter of maximum rosette radius achieved by wild type and suppression lines. Measurements were made on different days once plants entered the four-true-leaf stage. FIG. 15 depicts a visual difference between wild type and suppression lines 32 days after sowing. Stems of the AtHrBP1 transgenic plants were more elongated than those of the wild type plants.

Example 19

[0192] The AtHrBP1 coding region, bases 17-871 of SEQ. ID. No. 2, was subcloned into binary vector pPZP212 and was under the control of the NOS promoter (see FIG. 16). Tobacco plants were transformed with this construct via an Agrobacteria mediated method. The Agrobacterium tumefaciens strain used was LBA4404.

Example 20

[0193] AtHrBP1p was overexpressed in tobacco plants under the control of the NOS promoter. FIG. 16 shows the construct used for tobacco transformation. Three high expression lines were chosen for further studies in the T2 generation. The AtHrBP1p-overexpressing lines were about 20-30% taller than wild type Xanthi NN plants (see FIG. 17). When infiltrated with purified harpin, the transgenic lines developed HR much faster than wild type plants. This is consistent with another experiment in which purified recombinant His-tagged AtHrBP1p, when co-infiltrated along with purified harpin, increased the sensitivity of tobacco plants to the harpin protein.

Example 21

[0194] 61-day-old wild type and AtHrBP1p-overexpressing Xanthi NN tobacco plants were inoculated with tobacco mosaic virus by rubbing tobacco mosaic virus (TMV) with diatomaceous earth on the upper surface of leaves. Lesions appeared 2 days after manual inoculation. The picture in FIG. 18A was taken 3 days after inoculation. The diameter of disease spots was measured. On average, the diameter of a lesion on leaves of transgenic plants was 33.4% less than that seen on wild type plants (FIG. 18B). Therefore, the surface area of lesions on transgenic plant leaves was about 44.3% of those of the wild type plants.

Example 22

[0195] 52-day-old wild type and two independent AtHrBP1p-overexpressing Xanthi NN tobacco plants were inoculated with Pseudomonas solanacearum by root cutting. Disease symptoms started 11 days after inoculation. Diseases symptoms in wild type plants progressed through the course of the study. However, as seen in FIG. 19, the transgenic lines remained relatively healthy. FIG. 19 shows representative wild type and AtHrBP1p-overexpressing transgenic line plants 44 days after Pseudomonas inoculation.

[0196] Although the invention has been described in detail for the purpose of illustration, it is understood that such details are solely for that purpose. The variations can be made therein by those skilled in the art without departing from the spirit of the scope of the invention which is defined by the following claims.

1 86 1 284 PRT Arabidopsis thaliana 1 Met Ala Thr Ser Ser Thr Phe Ser Ser Leu Leu Pro Ser Pro Pro Ala 1 5 10 15 Leu Leu Ser Asp His Arg Ser Pro Pro Pro Ser Ile Arg Tyr Ser Phe 20 25 30 Ser Pro Leu Thr Thr Pro Lys Ser Ser Arg Leu Gly Phe Thr Val Pro 35 40 45 Glu Lys Arg Asn Leu Ala Ala Asn Ser Ser Leu Val Glu Val Ser Ile 50 55 60 Gly Gly Glu Ser Asp Pro Pro Pro Ser Ser Ser Gly Ser Gly Gly Asp 65 70 75 80 Asp Lys Gln Ile Ala Leu Leu Lys Leu Lys Leu Leu Ser Val Val Ser 85 90 95 Gly Leu Asn Arg Gly Leu Val Ala Ser Val Asp Asp Leu Glu Arg Ala 100 105 110 Glu Val Ala Ala Lys Glu Leu Glu Thr Ala Gly Gly Pro Val Asp Leu 115 120 125 Thr Asp Asp Leu Asp Lys Leu Gln Gly Lys Trp Arg Leu Leu Tyr Ser 130 135 140 Ser Ala Phe Ser Ser Arg Ser Leu Gly Gly Ser Arg Pro Gly Leu Pro 145 150 155 160 Thr Gly Arg Leu Ile Pro Val Thr Leu Gly Gln Val Phe Gln Arg Ile 165 170 175 Asp Val Phe Ser Lys Asp Phe Asp Asn Ile Ala Glu Val Glu Leu Gly 180 185 190 Ala Pro Trp Pro Phe Pro Pro Leu Glu Ala Thr Ala Thr Leu Ala His 195 200 205 Lys Phe Glu Leu Leu Gly Thr Cys Lys Ile Lys Ile Thr Phe Glu Lys 210 215 220 Thr Thr Val Lys Thr Ser Gly Asn Leu Ser Gln Ile Pro Pro Phe Asp 225 230 235 240 Ile Pro Arg Leu Pro Asp Ser Phe Arg Pro Ser Ser Asn Pro Gly Thr 245 250 255 Gly Asp Phe Glu Val Thr Tyr Val Asp Asp Thr Met Arg Ile Thr Arg 260 265 270 Gly Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ala 275 280 2 1000 DNA Arabidopsis thaliana 2 tttttccttc tcaacaatgg cgacttcttc tactttctcg tcactactac cttcaccacc 60 agctcttctt tccgaccacc gttctcctcc accatccatc agatactcct tttctccctt 120 aactactcca aaatcgtctc gtttgggttt cactgtaccg gagaagagaa acctcgctgc 180 taattcgtct ctcgttgaag tatccattgg cggagaaagt gacccaccac catcatcatc 240 tggatcagga ggagacgaca agcaaattgc attactcaaa ctcaaattac ttagtgtagt 300 ttcgggatta aacagaggac ttgtggcgag tgttgatgat ttagaaagag ctgaagtggc 360 tgctaaagaa cttgaaactg ctgggggacc ggttgattta accgatgatc ttgataagct 420 tcaagggaaa tggaggctgt tgtatagtag tgcgttctct tctcggtctt taggtggtag 480 ccgtcctggt ctacctactg gacgtttgat ccctgttact cttggccagg tgtttcaacg 540 gattgatgtg tttagcaaag attttgataa catagcagag gtggaattag gagccccttg 600 gccatttccg ccattagaag ccactgcgac attggcacac aagtttgaac tcttaggcac 660 ttgcaagatc aagataacat ttgagaaaac aactgtgaag acatcgggaa acttgtcgca 720 gattcctccg tttgatatcc cgaggcttcc cgacagtttc agaccatcgt caaaccctgg 780 aactggggat ttcgaagtta cctatgttga tgataccatg cgcataactc gcggggacag 840 aggtgaactt agggtattcg tcattgctta attctcaaag ctttgacatg taaagataaa 900 taaatacttt ctgcttgatg cagtctcatg agttttgtac aaatcatgtg aacatataaa 960 tgcgctttat aagtaaatga gtgtcttgtt caatgaatca 1000 3 4260 DNA Arabidopsis thaliana 3 aattagaaaa attaacaacc aacatctagt tagaatattt aatttgcacc aatgtcttcg 60 agtatagtga aaaaaataga agatcgaata tcgaatagta cgtatagaat catctagatc 120 cattcgaact aacgtctact tttcttttcc agcattaaca tgtagcttgt cattagcatt 180 tacatgttgc aaataacaca aattgggaaa ttgaaagact aaaaaacctt gtacagcaga 240 tggtttaaca cgtggattca tggacacaaa cagaaaacgg cagaactaag cacaaaaacg 300 tcaactaagc atatcaaagc ttttaatgca agcctaatat aaacacaagt ggttatccat 360 aatctgttct taatctcttg cagtagttat cttttcatta ttcgcaattc gcaattctat 420 attcttatat ttcaacttgt tcttcttcca aattgtaatt atatctacat cgtcttagct 480 tgaccattat agctccagta ccaagttctc ttcttaactt taatatcagc tactattctc 540 atactgtaaa tatcttttgt tcaccaaaca tatatttcga accaaactgc taaaagctta 600 tcataaattg cagttctagc cacacaattt tgcagttcca accattaaat gccacaaaat 660 ttggacgatt tcttaagaca agaagaacat agcaaccaaa ccttattgat taaatatgaa 720 atgtctccat aaaactggga gatttcccca aataaagaga acacggcaaa tgttcacgta 780 atctccaaga tgaatgttta attttttctt tcagaaaaaa acaaaaaaac ttaactcaat 840 atagacaact agaatggata ccaactaagc aaaagaaatt caaaagacaa atatatattg 900 gatatgaagt tacattattt tcaaacttta tatactacta aaagcctaaa aatttgttct 960 aaaatgatat ccaaataaat ggaaggcatg aatgtcatat gactaaaaga gaaaaacaca 1020 cctgtatata agtattggat catgctgcct ccgagtgaca aaacatacga tgtgggtctt 1080 tattgggcca tacttaaatg gaaaaaggag aaaaaaaatt gggcaatgtc tatggtcgaa 1140 atttatatgt tttacatcaa taaaatcaat atttaatttt atatatgtgg gtcttaatct 1200 agtattatct acatagatta aaatcaaagt actgcatatg gtccataata atacaaccaa 1260 agcaaattaa aattttgtgg cacaaaacga catcatttta ctcagaaagt aatatgcaat 1320 ttcgtttacg cacacacgta tacgcgctaa taacccgtgg tgcttctcaa atcacataat 1380 aattaaagtc ttcttcttct tcttcttctc tacaaattat ctcactctct tcgttttttt 1440 ttccttctca acaatggcga cttcttctac tttctcgtca ctactacctt caccaccagc 1500 tcttctttcc gaccaccgtt ctcctccacc atccatcaga tactcctttt ctcccttaac 1560 tactccaaaa tcgtctcgtt tgggtttcac tgtaccggag aagagaaacc tcgctgctaa 1620 ttcgtctctc gttgaagtat ccattggcgg agaaagtgac ccaccaccat catcatctgg 1680 atcaggagga gacgacaagc aaattgcatt actcaaactc aaattacttg tgagtctgat 1740 tcaaaccaat cggtgaaatt ataagaaatt ggtttcgttt ctttggaatt agggtttata 1800 ttactgttaa gattcgatta tagagtgaat tttgggaaga tttttcagat ttgatttgtg 1860 atgtgttgtg ttgtgagaaa ttgcagagtg tagtttcggg attaaacaga ggacttgtgg 1920 cgagtgttga tgatttagaa agagctgaag tggctgctaa agaacttgaa actgctgggg 1980 gaccggttga tttaaccgat gatcttgata agcttcaagg gaaatggagg ctgttgtata 2040 gtagtgcgtt ctcttctcgg tctttaggtg gtagccgtcc tggtctacct actggacgtt 2100 tgatccctgt tactcttggc caggtaattc ttgaatcatt gctctgtttt tacccgtcaa 2160 gattcggttt ttcgggtaag ttgttgagga gtttatgtgc atggtctagt ctatcatcaa 2220 tagtcttgct tgagtttgaa tggggctgag ctaagaatct agctttctga ggttacaatt 2280 tggtaatgtc atcttatact cgaaagcaaa cttttttcta tattgtcaag tttatgtgta 2340 cggtctggtc tatcattggt agtctttgtt gagcttgaat ggtgaggagc ttagaatcta 2400 gcaatgtcat ctactcctta atcatttttt tctatattgc caagtttatg tgtacggtct 2460 tagtcaatca tctttattct tggttgagtt tgaatggtga tgagcttaga atctagcttt 2520 ctttggttta aatttggcaa agaaccatac ctgaatcggt agaaagcaaa cttctttaat 2580 attatctctt gtttctgaat cattaaaaca ggtgtttcaa cggattgatg tgtttagcaa 2640 agattttgat aacatagcag aggtggaatt aggagcccct tggccatttc cgccattaga 2700 agccactgcg acattggcac acaagtttga actcttaggt ttgcatttcc ctttctctca 2760 ttaagtttat cgaattgtgt aagagcaaaa taacttatct gtatctttga catttatggg 2820 gaaaacaggc acttgcaaga tcaagataac atttgagaaa acaactgtga agacatcggg 2880 aaacttgtcg cagattcctc cgtttgatat cccgaggctt cccgacagtt tcagaccatc 2940 gtcaaaccct ggaactgggg atttcgaagt tacctatgtt gatgatacca tgcgcataac 3000 tcgcggggac agaggtgaac ttagggtatt cgtcattgct taattctcaa agctttgaca 3060 tgtaaagata aataaatact ttctgcttga tgcagtctca tgagttttgt acaaatcatg 3120 tgaacatata aatgcgcttt ataagtaaat gagtgtcttg ttcaatgaat catatgaaag 3180 aatttgtatg actcagaaaa ttggacaatg atatagacct tccaaatttt gcaccctcta 3240 atgtgagata ttagtgattt tttcttaggt tggtagagag aacggattgg caaaaaaata 3300 tcgaaggtca atgattaaca gcaaaaccat atcttgatga ttcaaaatat agagttaaca 3360 agcaaagatg agacaatctt atacgagaga gctaaaacaa atggattcca aatccagcaa 3420 gtacaaaaat cgcagaaaat aagatgaaac caacttaaaa cagagatgtt ccctttccct 3480 tcttgtcacc accgatctcg aaatgcttgc acctctgaaa taaacaacaa accaacacaa 3540 tgtaagcaaa ttaccaagtt acaaatccgg tataatgaac tgatctatgt tctatgcacc 3600 ttgataggac gctgcgaaaa gtgcttgcag ctttgacact gaagcctcaa aacaatcttc 3660 ttcgtggtct tagcctgtta acaagattca caagatgtat ctcagtccaa aactgagact 3720 attggaatgt ctgtttcctc acagctcact tccaaaattc tactataaat ggttccttaa 3780 aactacctca tttcaactaa ctagacctaa ttcaaactga aaaaacaatc aatgcatgat 3840 aatcaatgtt acctttttgt ggaagacagg cttagtctga ccaccataac cagattgttt 3900 acggtcataa cgacgctttc cttgagcagc aagactgtct ttacccttct tgtattgggt 3960 aaccttgtgc aaagtatgct ttttgcattc cttgttctta cagtaagtgt tctttgtctt 4020 tggaatgttc accttcaaaa ttcataaaat caaaaatgaa tcactcacac acatacaaaa 4080 tcaagagact tttaaggtta atcaaaatac aaacatcatt tagattgaaa acttttatga 4140 tagatctgaa aaacaataca ataaatcaat caaccatgta ttgttgttct tcaaagtcaa 4200 cgaactttac aaattccaaa atcacatcga aagagaagaa acaatttacc attttcgcgt 4260 4 203 PRT Oryza sativa 4 Val Ala Ala Leu Lys Val Lys Leu Leu Ser Ala Val Ser Gly Leu Asn 1 5 10 15 Arg Gly Leu Ala Gly Ser Gln Glu Asp Leu Asp Arg Ala Asp Ala Ala 20 25 30 Ala Arg Glu Leu Glu Ala Ala Ala Gly Gly Gly Pro Val Asp Leu Glu 35 40 45 Arg Asp Val Asp Lys Leu Gln Gly Arg Trp Arg Leu Val Tyr Ser Ser 50 55 60 Ala Phe Ser Ser Arg Thr Leu Gly Gly Ser Arg Pro Gly Pro Pro Thr 65 70 75 80 Gly Arg Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln Arg Ile Asp 85 90 95 Val Val Ser Lys Asp Phe Asp Asn Ile Val Asp Val Glu Leu Gly Ala 100 105 110 Pro Trp Pro Leu Pro Pro Val Glu Leu Thr Ala Thr Leu Ala His Lys 115 120 125 Phe Glu Ile Ile Gly Thr Ser Ser Ile Lys Ile Thr Phe Asp Lys Thr 130 135 140 Thr Val Lys Thr Lys Gly Asn Leu Ser Gln Leu Pro Pro Leu Glu Val 145 150 155 160 Pro Arg Ile Pro Asp Asn Leu Arg Pro Pro Ser Asn Thr Gly Ser Gly 165 170 175 Glu Phe Glu Val Thr Tyr Leu Asp Gly Asp Thr Arg Ile Thr Arg Gly 180 185 190 Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ser 195 200 5 613 DNA Oryza sativa 5 cgtggctgcg ctcaaagtca agcttctgag cgcggtgtcc gggctgaacc gcggcctcgc 60 ggggagccag gaggatcttg accgcgccga cgcggcggcg cgggagctcg aggcggcggc 120 gggtggcggc cccgtcgacc tggagaggga cgtggacaag ctgcaggggc ggtggaggct 180 ggtgtacagc agcgcgttct cgtcgcggac gctcggcggc agccgccccg gcccgcccac 240 cggccgcctc ctccccatca ccctcgggca ggtgtttcag aggatcgatg ttgtcagcaa 300 ggacttcgac aacatcgtcg atgtcgagct cggcgcgcca tggccgctgc cgccggtgga 360 gctgacggcg accctggctc acaagtttga gatcatcggc acctcgagca taaagatcac 420 attcgacaag acgacggtga agacgaaggg gaacctgtcc cagctgccgc cgctggaggt 480 ccctcgcatc ccggacaacc tccggccgcc gtccaacacc ggcagcggcg agttcgaggt 540 gacctacctc gacggcgaca cccgcatcac ccgcggggac agaggggagc tcagggtgtt 600 cgtcatctcg tga 613 6 277 PRT Gossypium 6 Met Ala Ser Ser Ser Phe Leu Leu Glu Ser Pro Ala Ser Ile Phe Ser 1 5 10 15 Ser Ser Ser Ile Lys Ala His Leu Tyr Leu Pro Lys Pro Tyr Pro Phe 20 25 30 Ile Val Ser Val Lys Arg Arg Arg Ser Glu Arg Lys Arg Asn Pro Val 35 40 45 Leu Lys Ser Ala Val Gly Asp Val Ser Val Val Asp Thr Pro Pro Pro 50 55 60 Pro Pro Pro Pro Pro Gln Asp Ala Lys Ser Glu Leu Ile Ser Ser Leu 65 70 75 80 Lys Leu Lys Leu Leu Gly Ile Val Ser Gly Leu Asn Arg Gly Leu Ala 85 90 95 Ala Asn Gln Asp Asp Leu Gly Lys Ala Asp Asp Ala Ala Lys Glu Leu 100 105 110 Glu Thr Val Ala Gly Pro Val Asp Leu Leu Thr Asp Leu Asp Lys Leu 115 120 125 Gln Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Ser Arg Thr 130 135 140 Leu Gly Gly Ser Arg Pro Gly Leu Pro Thr Gly Arg Leu Leu Pro Val 145 150 155 160 Thr Leu Gly Gln Val Phe Gln Arg Ile Asp Val Ile Ser Lys Asp Phe 165 170 175 Asp Asn Ile Ala Glu Ile Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro 180 185 190 Leu Glu Val Thr Ala Thr Leu Ala His Lys Phe Glu Ile Ile Gly Ser 195 200 205 Ser Lys Ile Lys Ile Thr Phe Glu Lys Thr Ser Val Lys Thr Arg Gly 210 215 220 Thr Phe Ser Gln Leu Pro Ser Leu Asp Val Pro Arg Ile Pro Asp Ala 225 230 235 240 Leu Arg Pro Pro Ser Asn Pro Gly Ser Gly Asp Phe Asp Val Thr Phe 245 250 255 Ile Asp Ala Asp Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg 260 265 270 Val Phe Val Ile Ser 275 7 1064 DNA Gossypium 7 aaagctttct tgcaaaaagc tccgaaaaag ggccagcaaa agccacttga gagccaatgg 60 cttcttcaag ttttcttcta gaatctccgg cgtctatctt ctcttcttcc tccattaaag 120 ctcatctcta tctcccgaaa ccctaccctt ttattgttag cgtgaaacgg cgccgttcgg 180 aaaggaagcg aaaccctgtt ttaaaatcgg ctgttggaga tgtctccgtc gttgacaccc 240 caccgccgcc gccgcctcca cctcaagatg ctaaatctga actcatttct tctttgaagc 300 ttaaattact gggtattgtt tctgggctga atagaggtct tgctgcgaac caagatgatc 360 tcggaaaagc agatgatgcc gccaaggaac tcgaaacggt tgctggacct gtggacttat 420 tgaccgatct tgataagctg caagggagat ggaaactgat atacagcagt gcattctcgt 480 ctcgtacact cggcgggagc cgtcctggac ttcccactgg aaggttgctc cctgtaactc 540 tcggccaggt ttttcagaga attgatgtca taagcaaaga ttttgataat atagcagaaa 600 ttgaattggg agctccatgg ccattacctc cacttgaagt tactgctacc ttagctcaca 660 aatttgaaat cataggatct tcaaagatca aaataacatt cgagaaaacg agtgtgaaaa 720 ctagagggac cttttctcag cttccgtcat tggatgtacc tcggattccc gacgctttga 780 ggcctccatc taatccaggg agcggcgact ttgatgttac cttcattgat gccgataccc 840 gaatcaccag aggagataga ggtgagctta gggtttttgt catctcataa attagtaagc 900 acatctaata tcaaagctcg tatgcactct cattacttca tatattgtct gtatgtgtat 960 atatcattgg gggtgatccg taactttttg tagaattaat attttaatgt aattacgaat 1020 attatgtatg taaattttcg aatcaattta atagtttaat cgtg 1064 8 265 PRT Glycine max 8 Met Ala Ser Leu Asn Leu Leu Pro His Pro Pro Leu Phe Ser Ser Phe 1 5 10 15 Leu His Arg Pro His Cys Asn Thr His Leu Leu Leu Thr Pro Lys Pro 20 25 30 Ser Gln Arg Arg Pro Ser Leu Val Val Lys Ser Thr Val Gly Val Ala 35 40 45 Asp Pro Ser Pro Ser Ser Ser Ser Tyr Ala Gly Asp Thr Ser Asp Ser 50 55 60 Ile Ser Ser Leu Lys Leu Asn Leu Leu Ser Ala Val Ser Gly Leu Asn 65 70 75 80 Arg Gly Leu Ala Ala Ser Glu Asp Asp Leu Arg Lys Ala Asp Asp Ala 85 90 95 Ala Lys Glu Leu Glu Ala Ala Gly Gly Leu Val Asp Leu Ser Leu Gly 100 105 110 Leu Asp Asn Leu Gln Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe 115 120 125 Ser Ser Arg Thr Leu Gly Gly Ser Arg Pro Gly Pro Pro Ile Gly Arg 130 135 140 Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln Arg Ile Asp Ile Leu 145 150 155 160 Ser Lys Asp Phe Asp Asn Ile Val Glu Leu Gln Leu Gly Ala Pro Trp 165 170 175 Pro Leu Pro Pro Leu Glu Ala Thr Ala Thr Leu Ala His Lys Phe Glu 180 185 190 Leu Ile Gly Ser Ser Lys Ile Lys Ile Val Phe Glu Lys Thr Thr Val 195 200 205 Lys Thr Ala Gly Asn Leu Ser Gln Leu Pro Pro Leu Glu Val Pro Arg 210 215 220 Ile Pro Asp Ala Leu Arg Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe 225 230 235 240 Glu Val Thr Tyr Leu Asp Ser Asp Thr Arg Ile Thr Arg Gly Asp Arg 245 250 255 Gly Glu Leu Arg Val Phe Val Ile Ala 260 265 9 1075 DNA Glycine max 9 ggcacgaggc tccaatccat ggcttccctg aacctccttc cccaccctcc acttttctct 60 tctttccttc acagaccaca ctgcaacacc catcttcttc tcacaccaaa accttctcaa 120 cgaaggcctt ctcttgtggt caaatctact gtgggtgtgg ctgacccttc tccatcttct 180 tcttcctacg ctggggatac ctctgattcc atctcttctt tgaagctcaa tctgctgagt 240 gctgtttctg ggctaaatag aggccttgct gcaagcgaag acgatcttcg aaaggcagat 300 gatgctgcta aggaacttga agctgctgga ggacttgtgg atctctcgct tggtcttgac 360 aatttgcaag gaagatggaa actcatttat agcagcgcat tttcgtctcg aacccttggt 420 ggaagccgtc ctggtcctcc cataggaaga ctccttccta ttactcttgg acaggttttt 480 caacgaattg acatcttgag caaagatttt gataacatag tggagcttca actaggtgct 540 ccatggcccc taccacccct tgaagcgact gccacattag ctcacaaatt tgaactcata 600 ggatcttcaa agataaagat agtatttgag aaaaccactg tgaagacagc tgggaatttg 660 tcacagttgc caccattgga ggtgcctcgg attcccgatg cattgaggcc tccatctaat 720 acgggaagcg gtgaatttga agttacatat cttgactcgg atactcgcat cacaagagga 780 gacagaggcg agctaagggt ctttgtgatt gcttgagttc ctggtgaatg caactatgca 840 ctatgcattt tctctgttgg acttaaaaaa aaaaggtttc aacaccttgt gccatcattt 900 tgtttagttt tttcctcctg atggtatttg ttctaagttc ttcaatattg taaacatgat 960 ggaattaaac tctactatat agttccaagg aagcagggta ctttttgttt aagtgtaaca 1020 tatttctttt ttaaggaata attgcttaca gatcattaga tatggatact tgaat 1075 10 276 PRT Hordeum vulgare 10 Met Ala Met Ala Ser Pro Ser Trp Ser Ser Cys Cys Thr Ser Thr Ser 1 5 10 15 Thr His Ser Leu Pro Gly Pro Pro Ala Ser Ser Lys Gly Arg Asn Pro 20 25 30 Trp Arg Ala Ser Ser Gly Arg Arg Ser Ala Ser Gly Gly Lys Arg Gln 35 40 45 Gln Lys Leu Ser Ile Arg Ala Val Ala Ala Pro Ser Ala Ala Val Asp 50 55 60 Tyr Ser Asp Thr Gly Ala Gly Ala Gly Asp Ile Pro Ser Lys Ile Lys 65 70 75 80 Leu Leu Ser Ala Val Ala Gly Leu Asn Arg Gly Leu Ala Ala Ser Gln 85 90 95 Glu Asp Leu Asp Arg Ala Asp Ala Ala Ala Arg Gln Leu Glu Ala Ala 100 105 110 Ala Pro Ala Pro Val Asp Leu Ala Lys Asp Leu Asp Lys Leu Gln Gly 115 120 125 Arg Trp Arg Leu Val Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly 130 135 140 Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu 145 150 155 160 Gly Gln Val Phe Gln Arg Ile Asp Val Val Ser Gln Asp Phe Asp Asn 165 170 175 Ile Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Val Glu 180 185 190 Ala Thr Ala Thr Leu Ala His Lys Phe Glu Ile Thr Gly Ile Ala Ser 195 200 205 Ile Lys Ile Asn Phe Asp Lys Thr Thr Val Lys Thr Asn Gly Asn Leu 210 215 220 Ser Gln Leu Pro Leu Leu Glu Val Pro Arg Ile Pro Asp Ser Leu Arg 225 230 235 240 Pro Pro Thr Ser Asn Thr Gly Ser Gly Glu Phe Asn Val Thr Tyr Leu 245 250 255 Asp Asp Asp Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg Val 260 265 270 Phe Val Val Thr 275 11 1129 DNA Hordeum vulgare 11 gccggtcggc acccaactgg aggttcagtt tcctcgttgc tctcctccat tgattgaccg 60 cctccttccc tgaggcgcac ggtacacgga cggcacccat ggccatggca tcgccgtcgt 120 ggtcatcctg ctgcacctca acctccaccc attctctgcc cggtcctccc gcgagcagcc 180 agggcaggaa cccgtggcgg gcaagcagcg gcaggaggag cgccagcgga gggaagaggc 240 agcagaagct gtccatccgc gcggtggccg caccgtcggc cgcggtggac tactcggaca 300 ccggcgccgg cgccggcgac atcccctcgc tgaaaatcaa gctgccgagc gccgtcgccg 360 ggctgaaccg gggcctcgct gcgagccagg aggacctgga ccgggcggac gcggcggcgc 420 ggcagctcga ggcggcggcg ccggcccccg tggacctcgc caaggatctc gacaagctgc 480 aggggcggtg gaggctggtc tacagcagcg ccttctcgtc gcggacgctc ggcggcagcc 540 gccccggccc gcccaccggt cgcctcctcc ccatcaccct cggccaggtg ttccagagga 600 tcgacgtggt gagccaggac ttcgacaaca tcgtggagct cgagctcggc gccccgtggc 660 cgctgccgcc ggtggaggcc acggccacgc tggcacacaa gtttgagatc accggaatcg 720 cgagtatcaa gatcaatttc gacaagacga cggtgaagac gaacgggaac ctgtcccagc 780 tgccgctgct ggaggtgccc cgcatcccgg atagcctcag gccgccgact tccaacaccg 840 ggagcggcga gttcaacgtg acctatctcg acgacgacac ccgcatcacc cgaggggaca 900 ggggggagct cagggtgttc gtcgtcacat gagctttttt ttgctgcgat ctctctcttt 960 gtagtgctcc aacttttttt ggcccgtaaa acaagagtct tgtactagtt ctatatatgc 1020 cttttgtttt ggggttcacc cgtccatccg cgggaaacat ctatcgtgac gactgttcga 1080 tgtataagcg gagtcgtccg atttacgcgg ttccgtcgtc ttttcgaac 1129 12 276 PRT Lycopersicon esculentum 12 Met Ala Ser Leu Leu His Ser Arg Leu Pro Leu Ser His Asn His Ser 1 5 10 15 Leu Ser Asn Ser Cys Gln Ser Phe Pro Cys His Leu Pro Gly Arg Ser 20 25 30 Lys Arg Ser Thr Gln Arg Leu Leu Glu Glu Arg Ser Tyr Asp Ser Lys 35 40 45 Arg Ser Leu Val Cys Gln Ser Gly Ile Asp Glu Val Thr Phe Ile Glu 50 55 60 Pro Pro Gly Ser Lys Glu Ala Glu Ala Glu Leu Ile Gly Ser Leu Lys 65 70 75 80 Leu Lys Leu Leu Ser Ala Val Ser Gly Leu Asn Arg Gly Leu Ala Ala 85 90 95 Ser Glu Asp Asp Leu Lys Lys Ala Asp Glu Ala Ala Lys Glu Leu Glu 100 105 110 Ser Cys Ala Gly Ala Val Asp Leu Ala Ala Asp Leu Asp Lys Leu Gln 115 120 125 Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu 130 135 140 Gly Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr 145 150 155 160 Leu Gly Gln Val Phe Gln Arg Ile Asp Val Leu Ser Lys Asp Phe Asp 165 170 175 Asn Ile Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Phe Pro Pro Val 180 185 190 Glu Ala Thr Ala Thr Leu Ala His Lys Phe Glu Leu Ile Gly Ser Ser 195 200 205 Thr Ile Lys Ile Ile Phe Glu Lys Thr Thr Val Lys Thr Thr Gly Asn 210 215 220 Leu Ser Gln Leu Pro Pro Leu Glu Val Pro Arg Ile Pro Asp Gln Phe 225 230 235 240 Arg Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe Glu Val Thr Tyr Ile 245 250 255 Asp Ser Asp Thr Arg Val Thr Arg Gly Asp Arg Gly Glu Leu Arg Val 260 265 270 Phe Val Ile Ser 275 13 1026 DNA Lycopersicon esculentum 13 tcgatccttt ttctgaaatt caagctcaac catggcttct ctacttcatt cgagacttcc 60 cctttctcac aatcattctt tatcaaattc ttgccaatct ttcccatgtc atctcccagg 120 aagaagcaag agaagtactc aaagattatt agaggaaagg agctatgaca gcaagagaag 180 tttagtttgc cagtcgggta ttgatgaagt cacttttatt gagccacctg gtagtaaaga 240 agctgaagcg gagcttattg ggtctctcaa actcaagtta ttgagtgctg tttctgggct 300 aaacagaggt cttgctgcaa gtgaagatga tctaaagaag gcggatgagg ctgccaagga 360 gctagaatct tgtgcaggag ctgtagatct cgcagctgat cttgataaac ttcaagggag 420 gtggaaattg atatacagca gtgcattctc atctcgtact cttggtggaa gtcgtcctgg 480 accccccact ggaagacttc ttcccatcac tcttggtcag gtatttcaaa gaatcgatgt 540 actgagcaaa gattttgaca acatagtgga gcttgaatta ggtgctccgt ggcctttccc 600 gcctgttgaa gcaactgcca ctttagccca caaatttgaa cttataggat catctacgat 660 taagattata ttcgagaaaa ctacagtgaa gacaactgga aatttatcac agctcccacc 720 attagaagtg cctcgcatac cagatcagtt caggccacca tcaaatacag gaagtggtga 780 gtttgaagtt acctacatcg attctgatac acgagtaaca aggggagaca gaggagagct 840 tagagttttc gttatctcat aagttaagct gcaatgaata tagtcttcct acaatgtttt 900 gttgctacaa tttcatgtaa caacatatca aatgtgtaga tatgctcaac attattctgc 960 tggtcacagc tatcaaatct gtaatgctac tgcaaattca aatctgtata cagtaaattt 1020 gacatc 1026 14 270 PRT Oryza sativa 14 Met Ala Ala Ala Val Ala Ser Ser Cys Cys Ala Ser Thr Ser Ala Arg 1 5 10 15 Pro Leu Val Arg Arg Ala Gly Ser Arg Asn Gly Lys Leu Trp Trp Ala 20 25 30 Gly Gly Val Arg Lys Ala Arg Leu Leu Ser Ile Ser Ala Thr Ala Ala 35 40 45 Ala Pro Ser Gly Val Asp Tyr Ala Ala Gly Thr Gly Ala Ala Ala Asp 50 55 60 Asp Asp Ala Val Ala Ala Leu Lys Val Lys Leu Leu Ser Ala Val Ser 65 70 75 80 Gly Leu Asn Arg Gly Leu Ala Gly Ser Gln Glu Asp Leu Asp Arg Ala 85 90 95 Asp Ala Ala Ala Arg Glu Leu Glu Ala Ala Ala Gly Gly Gly Pro Val 100 105 110 Asp Leu Glu Arg Asp Val Asp Lys Leu Gln Gly Arg Trp Arg Leu Val 115 120 125 Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly Gly Ser Arg Pro Gly 130 135 140 Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln 145 150 155 160 Arg Ile Asp Val Val Ser Lys Asp Phe Asp Asn Ile Val Asp Val Glu 165 170 175 Leu Gly Ala Pro Trp Pro Leu Pro Pro Val Glu Leu Thr Ala Thr Leu 180 185 190 Ala His Lys Phe Glu Ile Ile Gly Thr Ser Ser Ile Lys Ile Thr Phe 195 200 205 Asp Lys Thr Thr Val Lys Thr Lys Gly Asn Leu Ser Gln Leu Pro Pro 210 215 220 Leu Glu Val Pro Arg Ile Pro Asp Asn Leu Arg Pro Pro Ser Asn Thr 225 230 235 240 Gly Ser Gly Glu Phe Glu Val Thr Tyr Leu Asp Gly Asp Thr Arg Ile 245 250 255 Thr Arg Gly Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ser 260 265 270 15 1123 DNA Oryza sativa 15 tcgccattga ttttctctgt ctgctctgct gctcgcttgc ttgcgctgtc cggtttagct 60 ctgtctagct aggtagactg cggccatggc ggcggcggtg gcgtcgtctt gctgcgcctc 120 gaccagcgct cgcccactgg ttcgccgcgc cgggagcagg aacgggaagc tgtggtgggc 180 gggtggtgtc aggaaggcgc ggctgctgtc catctccgcc acggccgcgg cgccgtcggg 240 cgtggactac gcggcgggca ccggcgccgc cgccgacgac gacgccgtgg ctgcgctcaa 300 agtcaagctt ctgagcgcgg tgtccgggct gaaccgcggc ctcgcgggga gccaggagga 360 tcttgaccgc gccgacgcgg cggcgcggga gctcgaggcg gcggcgggtg gcggccccgt 420 cgacctggag agggacgtgg acaagctgca ggggcggtgg aggctggtgt acagcagcgc 480 gttctcgtcg cggacgctcg gcggcagccg ccccggcccg cccaccggcc gcctcctccc 540 catcaccctc gggcaggtgt ttcagaggat cgatgttgtc agcaaggact tcgacaacat 600 cgtcgatgtc gagctcggcg cgccatggcc gctgccgccg gtggagctga cggcgaccct 660 ggctcacaag tttgagatca tcggcacctc gagcataaag atcacattcg acaagacgac 720 ggtgaagacg aaggggaacc tgtcccagct gccgccgctg gaggtccctc gcatcccgga 780 caacctccgg ccgccgtcca acaccggcag cggcgagttc gaggtgacct acctcgacgg 840 cgacacccgc atcacccgcg gggacagagg ggagctcagg gtgttcgtca tctcgtgatc 900 ggacggacgc gttcgcgaca taggtatgcg gcttgcgatt ctgaaactga aactgaagcg 960 cacacacggt tttgtgttct ttctctgcta ctagtagatc ctcactctct tgatctgacc 1020 atctttgtac tatacttcag tattgttcgt gcgttctgta ttgttataga ttttgcagat 1080 attcaacaag tagagggaaa tatgtcaaaa tgagaaatcg agg 1123 16 269 PRT Oryza sativa 16 Met Ala Ala Ala Val Ala Ser Ser Cys Cys Ala Ser Thr Ser Ala Arg 1 5 10 15 Pro Leu Val Arg Arg Ala Gly Ser Arg Ser Gly Lys Leu Trp Trp Ala 20 25 30 Gly Gly Gly Arg Lys Ala Arg Leu Leu Ser Ile Ser Ala Thr Ala Ala 35 40 45 Ala Pro Ser Gly Val Asp Tyr Ala Ala Gly Thr Gly Ala Ala Asp Asp 50 55 60 Asp Ala Val Ala Ala Leu Lys Val Lys Leu Leu Ser Ala Val Ser Gly 65 70 75 80 Leu Asn Arg Gly Leu Ala Ala Ser Gln Glu Asp Leu Asp Arg Ala Asp 85 90 95 Ala Ala Ala Arg Glu Leu Glu Ala Ala Ala Gly Gly Gly Pro Val Asp 100 105 110 Leu Glu Gly Asp Met Asp Lys Leu Gln Gly Arg Trp Arg Leu Val Tyr 115 120 125 Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly Gly Ser Arg Pro Gly Pro 130 135 140 Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln Arg 145 150 155 160 Ile Asp Val Val Ser Lys Asp Phe Asp Asn Ile Val Asp Val Glu Leu 165 170 175 Gly Ala Pro Trp Pro Leu Pro Pro Val Glu Leu Thr Ala Thr Leu Ala 180 185 190 His Lys Phe Glu Ile Ile Gly Thr Ser Ser Ile Lys Ile Thr Phe Asp 195 200 205 Lys Thr Thr Val Lys Thr Lys Gly Asn Leu Ser Gln Leu Pro Pro Leu 210 215 220 Glu Val Pro Arg Ile Pro Asp Asn Leu Arg Pro Pro Ser Asn Thr Gly 225 230 235 240 Ser Gly Glu Phe Glu Val Thr Tyr Leu Asp Gly Asp Thr Arg Ile Thr 245 250 255 Arg Gly Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ser 260 265 17 1112 DNA Oryza sativa 17 tcgccattga ttttctctgt ctgctctgct gctcgcttgc ttgcgctgtc cggtttagct 60 ctgtctagct aggtagactg gcggccatgg cggcggcggt ggcgtcgtct tgctgcgcct 120 cgaccagcgc tcgcccactg gttcgccgcg ccgggagcag gagcgggaag ctgtggtggg 180 cgggtggtgg gaggaaggcg cggctgctgt ccatctccgc cacggccgcg gcgccgtcgg 240 gcgtggacta cgcggcgggc accggcgccg ccgacgacga cgccgtggct gcgctcaaag 300 tcaagcttct gagcgcggtg tccgggctga accgcggcct cgcggcgagc caggaggatc 360 ttgaccgggc cgacgcggcg gcgcgggagc tcgaggcggc ggcgggcggc gggcccgtcg 420 acctggaggg ggacatggac aagctgcagg ggcggtggag gctggtgtac agcagcgcgt 480 tctcgtcgcg gacgctcggc ggcagccgcc ccggcccgcc caccggccgc ctcctcccca 540 tcaccctcgg ccaggtgttt cagaggatcg atgttgtcag caaggacttc gacaacatcg 600 tcgatgtcga gctcggcgcg ccatggccgc tgccgccggt ggagctgacg gcgacgctgg 660 ctcacaagtt tgagatcatc ggcacctcga gcataaagat cacattcgac aagacgacgg 720 tgaagacgaa ggggaacctg tcccagctgc cgccgctgga ggtccctcgc atcccggaca 780 acctccggcc gccgtccaac accggcagcg gcgagttcga ggtgacctac ctcgacggcg 840 acacccgcat cacccgcggg gacagagggg agctcagggt gttcgtcatc tcgtgatcgg 900 acggacgcgt tcgcgacata ggtatgcggc ttgcgattct gaaactgaaa ctgaagcgca 960 cacacggttt tgtgttcttt ctctgctact agtagatcct cactctcttg atctgaccat 1020 ctttgtacta tacttcagta ttgttcgtgc gttctgtatt gttatagatt ttgcagatat 1080 tcaacaagta gagggaaata tgccaaaatg ag 1112 18 275 PRT Solanum tuberosum 18 Met Ala Ser Leu Leu His Ser Arg Leu Pro Leu Ser His Asn His Ser 1 5 10 15 Leu Ser Asn Ser Cys Gln Ser Phe Pro Cys His Leu Pro Gly Arg Ser 20 25 30 Lys Arg Ser Thr Gln Arg Phe Phe Glu Glu Arg Ser Tyr Asp Ser Lys 35 40 45 Arg Ala Leu Ile Cys Gln Ser Gly Ile Asp Glu Val Thr Phe Arg Leu 50 55 60 Pro Gly Ser Lys Glu Ala Lys Ala Glu Leu Ile Gly Ser Leu Lys Leu 65 70 75 80 Lys Leu Leu Ser Ala Val Ser Gly Leu Asn Arg Gly Leu Ala Ala Ser 85 90 95 Glu Asp Asp Leu Lys Lys Ala Asp Glu Ala Ala Lys Glu Leu Glu Ser 100 105 110 Cys Ala Gly Ala Val Asp Leu Ala Ala Asp Leu Asp Lys Leu Gln Gly 115 120 125 Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly 130 135 140 Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu 145 150 155 160 Gly Gln Val Phe Gln Arg Ile Asp Val Leu Ser Lys Asp Phe Asp Asn 165 170 175 Ile Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Phe Pro Pro Val Glu 180 185 190 Ala Thr Ala Thr Leu Ala His Lys Phe Glu Leu Ile Gly Ser Ser Thr 195 200 205 Ile Lys Ile Val Phe Glu Lys Thr Thr Val Lys Thr Thr Gly Asn Leu 210 215 220 Ser Gln Leu Pro Pro Ile Glu Val Pro Arg Ile Pro Asp Gln Phe Arg 225 230 235 240 Pro Pro Ser Asn Thr Gly Asn Gly Glu Phe Glu Val Thr Tyr Ile Asp 245 250 255 Ser Asp Thr Arg Val Thr Arg Gly Asp Arg Gly Glu Leu Arg Val Phe 260 265 270 Val Ile Ser 275 19 1078 DNA Solanum tuberosum unsure (1073) N at position 1073 is A, C, T, or G 19 ctaccaccaa tcaaactcca caaaagatcg atcctttttc tgaaattcaa gctcaaccat 60 ggcttctcta cttcattcta gacttcccct ttctcacaat cattctttat caaattcttg 120 ccaatctttc ccctgtcatc tcccaggaag aagcaagaga agtactcaaa gattctttga 180 ggaaaggagc tatgatagca agagagcctt aatttgtcag tcgggtattg atgaagtcac 240 ttttaggcta cctggtagta aagaagctaa agctgagctt attgggtctc tcaaactcaa 300 gttattgagt gctgtttctg ggctaaacag aggtcttgct gcaagtgaag atgatctaaa 360 gaaggcggat gaggctgcca aggagctgga atcttgtgca ggagctgtag atctcgcagc 420 tgatcttgat aagcttcaag ggaggtggaa attgatatac agcagtgcat tctcatctcg 480 tactcttggt ggaagtcgtc ctggcccccc cactggaaga cttcttccca tcactcttgg 540 tcaggtattt caaagaattg atgtactaag caaggatttt gacaacatag tggagcttga 600 attaggtgct ccgtggcctt tcccacctgt tgaagcaact gccactttag cccacaaatt 660 tgaacttata ggatcatcta caattaagat tgtattcgaa aaactcagtg aagacaactg 720 gaaatttatc acagttgcca ccaatagaag tgcctccata ccagatcagt tcaggccacc 780 atcaaataca ggaaatggtg agtttgaagt tacctatatc gattctgata cacgtgtaac 840 aaggggagac agaggagagc ttagagtttt cgttatctca taagttaagc tgcaataaat 900 atagttttcc tacaatattt tgttgctaca atttcatgta acaacatatc naatgtatag 960 atatgctcaa cattattctg ctggtcaaag ctagcaaatt tgtaatgcta ctgcaaattc 1020 aaatctgtat acagtaaatt tgacatgtga tggagttatg cagtgagatt tcnanaat 1078 20 277 PRT Triticum 20 Met Ala Met Ala Ser Pro Ser Trp Ser Ser Cys Cys Ala Ser Thr Ser 1 5 10 15 Thr Arg Pro Leu Pro Ser Pro Pro Ala Ser Ser Lys Ser Arg Asn Pro 20 25 30 Trp Arg Ala Ser Ser Gly Arg Arg Ser Ala Ser Gly Gly Lys Arg Arg 35 40 45 Gln Gln Leu Ser Ile Arg Ala Val Ala Ala Pro Ser Ser Ala Val Asp 50 55 60 Tyr Ser Asp Thr Ala Ala Gly Ala Gly Asp Val Pro Ser Leu Lys Ile 65 70 75 80 Lys Leu Leu Ser Ala Val Ala Gly Leu Asn Arg Gly Leu Ala Ala Ser 85 90 95 Gln Glu Asp Leu Asp Arg Ala Asp Ala Ala Ala Arg Gln Leu Glu Ala 100 105 110 Ala Ala Pro Ala Pro Val Asp Leu Ala Lys Asp Leu Asp Lys Leu Gln 115 120 125 Gly Arg Trp Arg Leu Val Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu 130 135 140 Gly Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr 145 150 155 160 Leu Gly Gln Val Phe Gln Arg Ile Asp Val Val Ser Gln Asp Phe Asp 165 170 175 Asn Ile Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Val 180 185 190 Glu Ala Thr Ala Thr Leu Ala His Lys Phe Glu Ile Thr Gly Ile Ala 195 200 205 Ser Ile Lys Ile Asn Phe Asp Lys Thr Thr Val Lys Thr Lys Gly Asn 210 215 220 Leu Ser Gln Leu Pro Leu Leu Glu Val Pro Arg Ile Pro Asp Ser Leu 225 230 235 240 Arg Pro Thr Thr Ser Asn Thr Gly Ser Gly Glu Phe Asp Val Thr Tyr 245 250 255 Leu Asp Asp Gly Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg 260 265 270 Val Phe Val Val Ser 275 21 1056 DNA Triticum 21 gaattcggca cgagctgacc tcttgccggt cggcgcccaa ttgaaaattt cttttctttt 60 tgctctcctg atcgattgac tgcctcacgg acggtgccca tggccatggc atcgccgtcg 120 tggtcatctt gctgcgcctc cacctccacc cgtcctctgc ctagcccccc cgcgagcagc 180 aagagcagga acccatggcg ggcaagcagc ggcaggagga gcgccagcgg agggaagaga 240 cgacagcagc tgtccatccg cgcggtggcc gcaccgtcgt cggcggtgga ctactcggac 300 accgccgccg gcgccggcga cgtcccctcg ctgaaaatca agctgctgag cgcggtcgcc 360 gggctgaacc ggggcctcgc ggcgagccag gaggacctgg accgggcgga cgcggcggcg 420 aggcagctcg aggcggcggc accggccccc gtggacctcg ccaaggacct cgacaagctg 480 caggggcggt ggaggctggt ctacagcagc gccttctcgt cgcggacgct cggcggcagc 540 cgccccggcc cgcccaccgg ccgcctcctc cccatcaccc tcggccaggt gttccagagg 600 atcgacgtgg tcagccagga cttcgacaac atcgtggagc tcgagctcgg cgcgccgtgg 660 ccgctgccgc cggtcgaggc cacggccacg ctggcgcaca agtttgagat caccggaatc 720 gcgagtatca agatcaattt cgacaagacg acggtgaaga ccaaagggaa cctgtcccag 780 ctgcctctgc tggaggtgcc ccgcatcccg gatagcctcc ggcctacgac gtccaacacc 840 gggagcggcg agttcgacgt gacctacctc gacgacggca cccgcatcac ccgaggggac 900 aggggggagc tcagggtgtt cgtcgtctca tgagctgata ttttttttgt tgatgttgct 960 gctgctttct ctctccgtgt actgcttcaa cctttttgcc cctaaacaga agtcttgaac 1020 tagttctatg tctatttttg ccggagtagt atcgtg 1056 22 275 PRT Triticum 22 Met Ala Ala Pro Ser Trp Ser Ser Cys Cys Ala Ser Thr Ser Thr Arg 1 5 10 15 Pro Leu Pro Ser Pro Pro Ala Ser Ser Lys Gly Gly Asn Pro Trp Arg 20 25 30 Ala Ser Ser Gly Arg Arg Ser Ala Ser Gly Gly Lys Arg Gln Gln Gln 35 40 45 Leu Ser Ile Arg Ala Val Ala Ala Pro Ser Ser Ala Val Asp Tyr Ser 50 55 60 Asp Thr Gly Ala Gly Ala Ala Asp Val Pro Ser Leu Lys Ile Lys Leu 65 70 75 80 Leu Ser Ala Val Ala Gly Leu Asn Arg Gly Leu Ala Ala Ser Gln Glu 85 90 95 Asp Leu Asp Arg Ala Asp Ala Ala Ala Arg Gln Leu Glu Ala Ala Ala 100 105 110 Pro Ala Pro Val Asp Leu Ala Lys Asp Leu Asp Lys Leu Gln Gly Arg 115 120 125 Trp Arg Leu Val Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly Gly 130 135 140 Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu Gly 145 150 155 160 Gln Val Phe Gln Arg Ile Asp Val Val Ser Gln Asp Phe Asp Asn Ile 165 170 175 Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Val Glu Ala 180 185 190 Thr Ala Thr Leu Ala His Lys Phe Glu Ile Thr Gly Ile Ala Ser Ile 195 200 205 Lys Ile Asn Phe Asp Glu Thr Thr Val Lys Thr Asn Gly Asn Leu Ser 210 215 220 Gln Leu Pro Leu Leu Glu Val Pro Arg Ile Pro Asp Ser Leu Arg Pro 225 230 235 240 Pro Ala Ser Asn Thr Gly Ser Gly Glu Phe Asp Val Thr Tyr Leu Asp 245 250 255 Asp Asp Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg Val Phe 260 265 270 Val Ile Ala 275 23 1205 DNA Triticum 23 actagtgatt cgcggatcca tatgctgcgt ttgctggctt tgatgaaact cgtgctcgtc 60 tctgacctct ggccggtcgg cacccaactg aaaatatctt ttctcgttgc tctcctcgat 120 cgattgactg cttcaccgga cggtgcccgt ggccatggca gcgccgtcgt ggtcatcttg 180 ctgcgcctcc acctccaccc gtcctctgcc tagccctccc gcgagcagca agggcgggaa 240 cccatggcgg gcaagcagcg gcaggaggag cgccagcgga gggaagaggc agcagcagct 300 gtccatccgc gcggtggccg cgccgtcgtc ggcggtggac tactcggaca ccggcgccgg 360 cgccggcgac gtcccctcgc tgaaaatcaa gctgctgagc gcggtggccg ggctgaaccg 420 gggcctcgcg gcgagccagg aggacctgga ccgggcggac gcggcggcga ggcagctcga 480 ggcggcggcg ccggcccccg tggacctcgc caaggacctc gacaagctgc aggggcggtg 540 gaggctggtc tacagcagcg ccttctcgtc gcggacgctc ggcggtagcc gccccggccc 600 gcccaccggc cgcctgctcc ccatcaccct cggccaggtg ttccagagga tcgacgtggt 660 gagccaggac ttcgacaaca tcgtggagct cgagctcggc gcgccgtggc cgctgccgcc 720 ggtggaggcc acggccacgc tggcacacaa gtttgagatc accgggatcg cgagtatcaa 780 gatcaatttc gacgagacga cggtgaagac gaatgggaac ctgtcccagc tgcctctgct 840 ggaggtgccc cgcatcccgg atagcctccg gccgccggcg tccaacaccg ggagcggcga 900 gttcgacgtg acctacctcg acgacgacac ccgcatcacc cgaggggaca ggggggagct 960 cagggtgttc gtcatcgcat gagcttgatc tttgcttgag atctctgtct ctgtactgct 1020 tcactttttt tgccccgaaa cagaagtctt tgtctagttc tatgtcttct tttgccggcg 1080 tagtattgtg atataggcta acgtgcgttc ttcacctatg ggattaactt tttctctcta 1140 gcagattatt acgtccggtt atttcgtttt ggttttatta tgttggctta agttttaatt 1200 atgtg 1205 24 272 PRT Zea mays 24 Met Ala Ala Thr Trp Ser Ser Ser Cys Cys Ala Ala Thr Ala Ser Ser 1 5 10 15 Ser Ala Leu Leu Arg His Ala Arg Val Lys Ser Ala Pro Trp Val Ala 20 25 30 Gly Ala Ser Arg Ser Ser Tyr Arg Gln Arg Arg Arg Arg Arg Glu Leu 35 40 45 Ser Ile Arg Ala Thr Ala Ala Ala Pro Pro Pro Pro Val Val Tyr Ala 50 55 60 Asp Ala Gly Ala Asp Asn Val Ala Ser Leu Lys Ile Lys Leu Leu Ser 65 70 75 80 Ala Val Ser Gly Leu Asn Arg Gly Leu Ala Ala Ser Gln Glu Asp Leu 85 90 95 Asp Arg Ala Asp Ala Ala Ala Arg Glu Leu Glu Ala Ala Ala Gly Cys 100 105 110 Pro Val Asp Leu Ser Arg Asp Leu Asp Lys Leu Gln Gly Arg Trp Arg 115 120 125 Leu Leu Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly Gly Ser Arg 130 135 140 Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu Gly Gln Val 145 150 155 160 Phe Gln Arg Ile Asp Val Val Ser Arg Asp Phe Asp Asn Ile Val Glu 165 170 175 Leu Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Leu Glu Ala Thr Ala 180 185 190 Thr Leu Ala His Lys Phe Glu Ile Ile Gly Thr Ser Gly Ile Lys Ile 195 200 205 Thr Phe Glu Lys Thr Thr Val Lys Thr Lys Gly Asn Leu Ser Gln Leu 210 215 220 Pro Pro Leu Glu Val Pro Arg Ile Pro Asp Asn Leu Arg Pro Pro Ser 225 230 235 240 Asn Thr Gly Ser Gly Glu Phe Glu Val Thr Tyr Leu Asp Asp Asp Thr 245 250 255 Arg Val Thr Arg Gly Asp Arg Gly Glu Leu Arg Val Phe Val Ile Ala 260 265 270 25 1218 DNA Zea mays 25 ccaccacaaa tattcttccc gccacgatcc ctctcatccg gaagaaaggg gaaaaaaact 60 cgcctttttc tctctgctgg ttcaagaacg ccatggaaga tctcgagcgc tcgctgtgat 120 tcctgcgagt acccaagccc aaccaagccc tggcccggca gccattctct tcgcgccaca 180 tcgcacgacc tccccgaagc agacgtgccc gctgcccgtc cgtcccccgt ggccatggcc 240 gcgacgtggt cttcgtcttg ctgcgccgcg accgcgtcga gcagcgctct gcttcgtcat 300 gcccgcgtca agagcgcgcc ttgggtagcc ggtgccagcc ggagtagcta caggcagcgg 360 cggcggcggc gggagctgtc catccgcgcc acggccgcgg cgccgccgcc gcccgtggtc 420 tacgcggacg ccggcgccga caacgtggcc tcgctgaaga tcaagctcct gagcgcggtg 480 tccgggctga accgtggcct ggcagcgagc caggaggacc tggaccgcgc ggacgcggcg 540 gcgcgggagc tggaggcggc ggcggggtgc cccgtcgacc tcagcaggga cctcgataag 600 ctgcagggcc ggtggcggct gctgtacagc agcgcgttct cttcgcggac gctcggcggc 660 agccgccttg gcccgcccac cggccgcctc ctccccatca cgctcggcca ggtgttccag 720 cggatcgacg tggtgagccg cgacttcgac aacatcgtgg agctggagct cggcgcgccg 780 tggcctctgc cgccgctcga ggccacggcg acgctggcgc acaagttcga gatcatcggg 840 acctcgggca tcaagatcac gttcgagaag acgacggtga agaccaaggg caacctgtcg 900 cagcttcctc cgctggaggt gccccgcatc ccggacaacc tccgcccccc gtccaacacc 960 gggagcggcg agttcgaggt gacctacctc gacgacgaca cgcgcgtcac ccgcggggac 1020 aggggggagc tcagggtgtt tgtcatcgcg tgacctgatc gcgcttcggc gccgttctgc 1080 tggtccgtga gattgccatc cttcttcctc cctgttgctc cagtagattt gttggtttct 1140 tcgtctgacc aatgtatacc gttctgttct tccgtgaact gaatctgcga ttaacttagt 1200 aactatcttg tgtggttt 1218 26 285 PRT Citrus paradisi 26 Met Ala Ser Leu Thr Leu Thr Pro Leu Phe His Ser Pro Thr Phe Leu 1 5 10 15 Ser Ser Asn Thr Asn Thr His Thr Val Thr Lys Lys Leu Ser Phe Pro 20 25 30 Ser Pro Thr Arg Arg Arg Leu Leu Val Asn Gly Lys Glu Tyr Arg Ser 35 40 45 Arg Arg Arg Ser Leu Val Leu Arg Arg Ser Ala Val Asp Asp Val Pro 50 55 60 Val Leu Asp Pro Pro Pro Pro Pro Pro Pro Asp Ser Ser Glu Ser Asp 65 70 75 80 Lys Thr Glu Leu Ile Ala Ser Leu Lys Leu Lys Leu Leu Ser Ala Val 85 90 95 Ser Gly Leu Asn Arg Gly Leu Ala Ala Asn Thr Asp Asp Leu Gln Lys 100 105 110 Ala Asp Ala Ala Ala Lys Glu Leu Glu Ala Val Gly Gly Pro Val Asp 115 120 125 Leu Ser Val Gly Leu Asp Arg Leu Gln Gly Lys Trp Arg Leu Leu Tyr 130 135 140 Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly Gly Asn Arg Pro Gly Pro 145 150 155 160 Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln Arg 165 170 175 Ile Asp Ile Leu Ser Lys Asp Phe Asp Asn Ile Ala Glu Leu Glu Leu 180 185 190 Gly Val Pro Trp Pro Leu Pro Pro Val Glu Val Thr Ala Thr Leu Ala 195 200 205 His Lys Phe Glu Leu Ile Gly Ser Ser Asn Ile Lys Ile Ile Phe Glu 210 215 220 Lys Thr Thr Val Lys Thr Thr Gly Asn Leu Ser Gln Leu Pro Pro Leu 225 230 235 240 Glu Leu Pro Arg Phe Pro Asp Ala Leu Arg Arg Pro Ser Asp Thr Arg 245 250 255 Ser Gly Glu Phe Glu Val Thr Tyr Leu Asp Asn Asp Thr Arg Ile Thr 260 265 270 Arg Gly Asp Arg Gly Glu Leu Arg Val Phe Val Ile Thr 275 280 285 27 1101 DNA Citrus paradisi 27 ttcgattgcc agacgctgcg tttgctggct ttgatgaaac ctctttcatt ccctgctggc 60 cacaaacaca cgccgacatt gaaactcccc ccacccacat catggcttct ctgactctaa 120 cccctctttt tcattcacca acatttcttt ccagcaatac taacacacac acagtcacaa 180 aaaaactgtc ttttccatct ccaacgcgac gtcgtctgct tgttaatggt aagagtatcg 240 aagtagaaga agaagccttg ttttgaggag gtcagccgtt gatgacgttc ctgttcttga 300 cccaccactc ctcctcctcc cgattcttca gaaagcgaca aaactgagct cattgcttct 360 ttgaagctca agttgcttag tgctgtttct gggctgaaca gaggtcttgc tgcaaacaca 420 gatgatctgc agaaggcaga cgctgctgca aaagagcttg aggctgttgg aggaccagta 480 gacctctcgg ttggtctcga tagactacaa gggaaatgga gactactgta cagcagtgca 540 ttctcatctc gcactctagg tggaaatcgg cctggacctc ccactggaag gctactcccc 600 ataactcttg gccaggtctt tcaacggatt gacatcttaa gcaaagattt tgataacata 660 gcagaacttg aattgggtgt tccatggccc ctgccaccag ttgaagtgac tgccacatta 720 gcccataaat ttgaactcat aggatcatca aatattaaaa taatatttga gaagacaact 780 gtaaagacaa cagggaactt atcacagctt ccaccccttg agttacctcg ttttccagat 840 gcattaaggc gtccatctga cacaagaagt ggtgaatttg aggtgacata cctcgataat 900 gatacccgca ttaccagagg agacagaggc gagctaagag ttttcgtgat cacttaggtt 960 ccttacatcc gtacagtttc cagcttgtat ctacattatt ttctgatgat tatatacaca 1020 aagtggtaaa aagaagcccc gtgaaaagca gttcttcctg gatcaagtga atcattgcac 1080 aattatatat ttttcatgcg c 1101 28 282 PRT Pyrus malus 28 Met Ala Met Ala Ser Leu Ser Ser Leu Pro His Ser Leu His Ser Ser 1 5 10 15 Pro Ser Thr Ser Ser Ala Asn Tyr Val Ile Pro Ser Lys Pro Pro Cys 20 25 30 Pro Lys Arg Leu Arg Phe Gly Ser Ser Asn Arg Arg His Thr Lys Ser 35 40 45 Phe Ala Pro Arg Ala Ala Val Asp Glu Val Ser Val Leu Glu Pro Pro 50 55 60 Pro Pro Gln Pro Pro Ser Ser Gly Ser Lys Thr Thr Pro Asn Pro Glu 65 70 75 80 Leu Val Ala Ser Leu Lys Leu Asn Leu Leu Ser Ala Val Ser Gly Leu 85 90 95 Asn Arg Gly Leu Ala Ala Ser Gly Glu Asp Leu Gln Lys Ala Glu Ala 100 105 110 Ala Ala Lys Glu Ile Glu Ala Ala Gly Gly Pro Val Asp Leu Ser Thr 115 120 125 Asp Leu Asp Lys Leu Gln Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala 130 135 140 Phe Ser Ser Arg Thr Leu Gly Gly Ser Arg Pro Gly Pro Pro Thr Gly 145 150 155 160 Arg Leu Leu Pro Ile Thr Leu Gly Gln Val Phe Gln Arg Ile Asp Ile 165 170 175 Phe Ser Lys Asp Phe Asp Asn Ile Val Glu Leu Glu Leu Gly Ala Pro 180 185 190 Trp Pro Leu Pro Pro Val Glu Ala Thr Ala Thr Leu Ala His Lys Phe 195 200 205 Glu Leu Ile Gly Ser Ser Arg Val Lys Ile Ile Phe Glu Lys Thr Thr 210 215 220 Val Lys Thr Thr Gly Asn Leu Ser Gln Leu Pro Pro Leu Glu Leu Pro 225 230 235 240 Lys Leu Pro Glu Gly Leu Arg Pro Pro Ser Asn Pro Gly Ser Gly Glu 245 250 255 Phe Asp Val Thr Tyr Leu Asp Ala Asp Ile Arg Ile Thr Arg Gly Asp 260 265 270 Arg Asp Glu Leu Arg Val Phe Val Val Ser 275 280 29 1138 DNA Pyrus malus 29 ggctttgatg aaatttcctt tctactttct agccatggcc atggcttctt tgagctctct 60 ccctcactct ctacattcct cgccttctac ttcttctgca aactatgtta ttccaagcaa 120 accaccctgc ccaaaacgcc tccgttttgg ttcgtcaaat cgccgtcaca ccaaaagctt 180 tgctccgaga gcagctgtgg acgaggtttc tgttctcgaa ccgccgccac cacagccgcc 240 gtcttccgga agcaaaacca cgcccaaccc tgaacttgta gcgtctttaa agctcaacct 300 attgagtgct gtttctgggc taaatagagg tcttgcagca tcgggagagg atctacaaaa 360 ggcagaagct gctgccaagg agattgaagc tgctggaggt ccagtggatc tctcaactga 420 tcttgataaa ctgcaaggga gatggaaatt gatatatagc agtgcatttt cttctcgtac 480 tctaggtggg agccgtcctg gacctcccac cggaaggcta ctcccaatta ccttaggcca 540 ggtatttcaa cggattgaca tcttcagcaa agactttgat aacatagtgg agcttgaact 600 aggtgctcca tggcccctgc cacccgttga agcaactgcc actttggccc acaaatttga 660 actcatagga tcttccaggg ttaagatcat ttttgagaaa actactgtga agactactgg 720 aaacttatcg cagcttcctc cattagagtt acctaagtta ccggaaggac tacgacctcc 780 gtctaaccca ggaagtggtg aatttgacgt tacctacctt gatgctgata tccgcatcac 840 aagaggagat agagacgagc taagggtttt tgttgtttca tagtttcttg ttagtttctt 900 ttcctacttc caatgtatct ccatctgttt tgccttgcgt cttcttggtg tcgtttgatc 960 atatgttgtt acttccaatt gttgtatgca tgaaccggtg gatggaagtt ccaggaaatg 1020 ttcaacgagg aacaacactg tatacatgta aattttgtaa tcgataaagt gaatcgtctt 1080 tgtcacttgg attgtatctg cattgccttt tcaagtgata tctatatgag ttttaggc 1138 30 276 PRT Nicotiana tabacum 30 Met Ala Ser Leu Leu Gln Tyr Ser Thr Leu Pro Leu Ser Asn Asn His 1 5 10 15 Cys Ser Ser Ser Leu Pro Ser Leu Thr Cys His Leu Ser Lys Arg Ser 20 25 30 Asn Arg Asn Thr Gln Lys Leu Leu Glu Lys Lys Lys Tyr His Ile Lys 35 40 45 Lys Ser Leu Ile Cys Gln Ser Gly Ile Asp Glu Leu Ala Phe Ile Glu 50 55 60 Leu Pro Gly Thr Lys Glu Ala Lys Ala Glu Leu Ile Gly Ser Leu Lys 65 70 75 80 Leu Lys Leu Leu Ser Ala Val Ser Gly Leu Asn Arg Gly Leu Ala Ala 85 90 95 Ser Glu Glu Asp Leu Lys Lys Ala Asp Ala Ala Ala Lys Glu Leu Glu 100 105 110 Ser Cys Ala Gly Ala Val Asp Leu Ser Ala Asp Leu Asp Lys Leu Gln 115 120 125 Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Gly Arg Thr Leu 130 135 140 Gly Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr 145 150 155 160 Leu Gly Gln Val Phe Gln Arg Ile Asp Val Leu Ser Lys Asp Phe Asp 165 170 175 Asn Ile Val Glu Leu Glu Leu Gly Ala Pro Trp Pro Leu Pro Pro Ala 180 185 190 Glu Leu Thr Ala Thr Leu Ala His Lys Phe Glu Leu Ile Gly Ser Ser 195 200 205 Thr Ile Lys Ile Thr Phe Glu Lys Thr Thr Val Lys Thr Thr Gly Ile 210 215 220 Leu Ser Gln Leu Pro Pro Phe Glu Val Pro Arg Ile Pro Asp Gln Leu 225 230 235 240 Arg Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe Glu Val Thr Tyr Ile 245 250 255 Asp Ser Asp Thr Arg Val Thr Arg Gly Asp Arg Gly Glu Leu Arg Val 260 265 270 Phe Val Ile Ser 275 31 1044 DNA Nicotiana tabacum 31 attcacaaac ctttccaaat attgagctga aattaaagct caacaatggc ttctctactt 60 cagtactcta cacttcctct ttctaataat cattgttcat cttcgttacc atctttaact 120 tgtcatctct caaaaagaag caatagaaat actcaaaaat tattagagaa aaagaagtat 180 catatcaaga aaagcttaat ttgccagtcg ggtattgatg aactcgcatt cattgagtta 240 cctggtacta aagaagctaa agctgaactt attgggtctc tcaaactcaa gttattgagt 300 gctgtttctg ggctaaacag aggtcttgct gcgagcgaag aagacctaaa gaaggcggat 360 gctgctgcca aggagctaga atcctgtgca ggagctgtag atctctcagc tgatctcgat 420 aaacttcaag ggaggtggaa attgatatac agcagtgcat tctcaggtcg cactcttgga 480 ggaagtcgtc ctggaccccc caccggaaga cttcttccca ttactcttgg tcaggtattt 540 caaagaattg atgtgctaag caaggatttt gacaacatag tggagcttga attaggtgct 600 ccttggcctt taccacctgc tgagttgact gccactttag cccacaaatt tgaactgata 660 ggatcatcca cgattaagat tacattcgag aaaactactg tgaagacaac cggaatctta 720 tcacagctcc caccatttga ggtgcctcgg ataccagatc aactcaggcc accatctaat 780 acaggaagtg gtgagtttga agttacctat attgattctg atacacgcgt aacaagggga 840 gacagaggag agcttagagt tttcgttatc tcataagatg gaatgcaata gatatagttt 900 tcctacaata ttttgttgct acaatttcat gtacaatata tcaaatgtat agatatgctc 960 aacattattc tgctggtcca tatctagcaa agttgtaatg ttactgcaaa tttgaatctg 1020 tatacagtaa actcgatttt gcga 1044 32 291 PRT Vitis 32 Met Thr Ser Leu Leu His Pro Leu Thr Ser Phe Ser Leu Ser Pro Ser 1 5 10 15 Pro Pro Pro Pro Leu Ser Ser Ser Ser Ser Ser Thr Ile Thr Ile Thr 20 25 30 Cys Ala Leu Pro Ser Asn Leu Arg Ser Ser Asp Arg Arg Arg Leu Arg 35 40 45 Thr Thr Ser Lys Pro Tyr Thr Trp Thr Ser Gly Leu Pro Lys Arg Ser 50 55 60 Phe Val Leu Arg Ser Thr Leu Asp Glu Val Ser Val Leu Asp Pro Pro 65 70 75 80 Pro Pro Pro Glu Asp Ser Thr Ala Asp Leu Leu Ser Ser Leu Lys Leu 85 90 95 Lys Leu Leu Ser Ala Val Ser Gly Leu Asn Arg Gly Leu Ala Ala Ile 100 105 110 Glu Asp Asp Leu Gln Lys Ala Asp Ala Ala Ala Lys Glu Leu Glu Ala 115 120 125 Ala Gly Gly Thr Val Asp Leu Ser Ile Asp Leu Asp Lys Leu Gln Gly 130 135 140 Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu Gly 145 150 155 160 Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr Leu 165 170 175 Gly Gln Val Phe Gln Arg Ile Asp Ile Val Ser Lys Asp Phe Asp Asn 180 185 190 Ile Val Asp Leu Gln Ile Gly Val Pro Trp Pro Leu Pro Pro Ile Glu 195 200 205 Leu Thr Ala Thr Leu Ala His Lys Phe Glu Leu Ile Gly Thr Ser Ser 210 215 220 Ile Lys Ile Thr Phe Glu Lys Thr Thr Val Lys Thr Thr Gly Asn Leu 225 230 235 240 Ser Gln Leu Pro Pro Leu Glu Val Pro Arg Ile Pro Asp Ala Leu Arg 245 250 255 Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe Glu Val Thr Tyr Leu Asp 260 265 270 Ala Asp Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg Val Phe 275 280 285 Val Ile Ala 290 33 1038 DNA Vitis 33 accgccagcc aactatgact tctctcctcc atcctctcac ctctttctcc ctttctccat 60 caccaccacc gcccctttct tcttcttctt cttctactat tactatcacg tgtgctcttc 120 ccagtaacct acgttcttca gaccgacgtc gtcttagaac aacatcaaaa ccttatacgt 180 ggacatcggg cctgcccaag agaagctttg tcctgaggtc aacccttgat gaggtctctg 240 ttcttgaccc ccctcctccc cctgaagact ccacggccga tcttctttcg tctctcaagc 300 tgaaactact gagtgctgtg tctggtctaa atagaggact tgctgcaatc gaggatgatc 360 ttcagaaggc agatgctgct gccaaagagc ttgaagctgc tggaggaact gttgacctct 420 caattgatct tgataaactt cagggaagat ggaaattgat atatagcagt gcgttctcat 480 cccgtactct aggtgggagc cgtcctggac ctcccactgg aaggctactc cctataactc 540 tgggccaggt atttcaaagg attgacattg taagcaaaga ttttgacaat atagtagatc 600 tccagatagg tgtcccatgg ccccttccgc caattgaact cactgccaca ttagcccaca 660 agtttgaact cataggaact tccagcatta aaataacatt cgagaaaaca actgtgaaga 720 caacaggaaa cctgtcgcag ctgccaccat tggaggtacc tcggatccca gatgcattga 780 ggccaccatc taatacagga agtggcgaat ttgaggttac ataccttgat gctgataccc 840 gcatcaccag aggagacagg ggtgagctta gagtttttgt cattgcataa actctaagca 900 ctcgtcacca tgactcacaa ttgaagaaaa taccatatcc aatccccttt tcttcttgtc 960 attttgtaaa cagtcccctg tttcttactg tttgtaggga acatgtcttg ttacatataa 1020 ctgtaaattc attttttt 1038 34 292 PRT Vitis 34 Met Thr Ser Leu Leu His Pro Leu Thr Ser Phe Ser Leu Ser Pro Ser 1 5 10 15 Pro Pro Pro Pro Leu Ser Phe Ser Ser Ser Ser Ser Thr Ile Thr Ile 20 25 30 Thr Cys Ala Leu Pro Ser Asn Leu Arg Ser Ser Asp Arg Arg Arg Leu 35 40 45 Arg Thr Thr Ser Lys Pro Tyr Thr Trp Thr Ser Gly Leu Pro Lys Arg 50 55 60 Ser Phe Val Leu Arg Ser Thr Leu Asp Glu Val Ser Val Leu Asp Pro 65 70 75 80 Pro Pro Pro Pro Glu Asp Ser Thr Ala Asp Leu Leu Ser Ser Leu Lys 85 90 95 Leu Lys Leu Leu Ser Thr Val Ser Gly Leu Asn Arg Gly Leu Ala Ala 100 105 110 Ile Glu Asp Asp Leu Gln Lys Ala Asp Ala Ala Ala Lys Glu Leu Glu 115 120 125 Ala Ala Gly Gly Thr Val Asp Leu Ser Ile Asp Leu Asp Lys Leu Gln 130 135 140 Gly Arg Trp Lys Leu Ile Tyr Ser Ser Ala Phe Ser Ser Arg Thr Leu 145 150 155 160 Gly Gly Ser Arg Pro Gly Pro Pro Thr Gly Arg Leu Leu Pro Ile Thr 165 170 175 Leu Gly Gln Val Phe Gln Arg Ile Asp Ile Val Ser Lys Asp Phe Asp 180 185 190 Asn Ile Val Asp Leu Gln Ile Gly Ala Pro Trp Pro Leu Pro Pro Ile 195 200 205 Glu Leu Thr Ala Thr Leu Ala His Lys Phe Glu Leu Ile Gly Thr Ser 210 215 220 Ser Ile Lys Ile Thr Phe Glu Lys Thr Thr Val Lys Thr Thr Gly Asn 225 230 235 240 Leu Ser Gln Leu Pro Pro Leu Glu Val Pro Arg Ile Pro Asp Ala Leu 245 250 255 Arg Pro Pro Ser Asn Thr Gly Ser Gly Glu Phe Glu Val Thr Tyr Leu 260 265 270 Asp Ala Asp Thr Arg Ile Thr Arg Gly Asp Arg Gly Glu Leu Arg Val 275 280 285 Phe Val Ile Ala 290 35 1055 DNA Vitis 35 accgccagcc aactatgact tctctcctcc atcctctcac ctctttctcc ctttctccat 60 caccaccacc gcccctttct ttttcttctt cttcttctac tattactatc acgtgtgctc 120 ttcccagtaa cctacgttct tcagaccgac gtcgtcttag aacaacatca aaaccttata 180 cgtggacatc gggcctgccc aagagaagct ttgtcctgag gtcaaccctt gatgaggtct 240 ctgttcttga cccccctcct ccccctgaag actccacggc cgatcttctt tcgtctctca 300 aactgaaact actgagtact gtgtctggtc taaatagagg acttgctgca atcgaggatg 360 atcttcagaa ggcagatgct gctgccaaag agcttgaagc tgctggagga actgttgacc 420 tctcaattga tcttgataaa cttcagggaa gatggaaatt gatatatagc agtgcgttct 480 catcccgtac tctaggtggg agccgtcctg gacctcccac tggaaggcta ctccctataa 540 ctctggggca ggtatttcaa aggattgaca ttgtaagcaa agattttgac aatatagtag 600 atctccagat aggtgcccca tggccccttc cgccaattga actcactgcc acattagccc 660 acaagtttga actcatagga acttccagca ttaaaataac attcgagaaa acaactgtga 720 agacaacagg aaacctgtcg cagcttccac cattggaggt acctcggatc ccagatgcat 780 tgaggccacc atctaataca ggaagtggcg aatttgaggt tacatacctt gatgctgata 840 cccgcatcac cagaggagac aggggtgagc ttagagtttt tgtcattgca taaactctac 900 actcgtcacc atgactcaca attgaagaaa atacaatatc caatcccctt ttcttcttgt 960 cattttgtaa actgtcccct gtttcttact gtttgtaggg aacatgtctt gttacataac 1020 tgtaaattca ttttttctac atttgatctt tacag 1055 36 26 PRT Xanthomonas campestris pv. glycines 36 Thr Leu Ile Glu Leu Met Ile Val Val Ala Ile Ile Ala Ile Leu Ala 1 5 10 15 Ala Ile Ala Leu Pro Ala Tyr Gln Asp Tyr 20 25 37 114 PRT Xanthomonas campestris pv. pelargonii 37 Met Asp Ser Ile Gly Asn Asn Phe Ser Asn Ile Gly Asn Leu Gln Thr 1 5 10 15 Met Gly Ile Gly Pro Gln Gln His Glu Asp Ser Ser Gln Gln Ser Pro 20 25 30 Ser Ala Gly Ser Glu Gln Gln Leu Asp Gln Leu Leu Ala Met Phe Ile 35 40 45 Met Met Met Leu Gln Gln Ser Gln Gly Ser Asp Ala Asn Gln Glu Cys 50 55 60 Gly Asn Glu Gln Pro Gln Asn Gly Gln Gln Glu Gly Leu Ser Pro Leu 65 70 75 80 Thr Gln Met Leu Met Gln Ile Val Met Gln Leu Met Gln Asn Gln Gly 85 90 95 Gly Ala Gly Met Gly Gly Gly Gly Ser Val Asn Ser Ser Leu Gly Gly 100 105 110 Asn Ala 38 342 DNA Xanthomonas campestris pv. pelargonii 38 atggactcta tcggaaacaa cttttcgaat atcggcaacc tgcagacgat gggcatcggg 60 cctcagcaac acgaggactc cagccagcag tcgccttcgg ctggctccga gcagcagctg 120 gatcagttgc tcgccatgtt catcatgatg atgctgcaac agagccaggg cagcgatgca 180 aatcaggagt gtggcaacga acaaccgcag aacggtcaac aggaaggcct gagtccgttg 240 acgcagatgc tgatgcagat cgtgatgcag ctgatgcaga accagggcgg cgccggcatg 300 ggcggtggcg gttcggtcaa cagcagcctg ggcggcaacg cc 342 39 205 DNA Arabidopsis thaliana 39 gatcaagata acatttgaga aaacaactgt gaagacatcg ggaaacttgt cgcagattcc 60 tccgtttgat atcccgaggc ttcccgacag tttcagacca tcgtcaaacc ctggaactgg 120 ggatttcgaa gttacctatg ttgatgatac catgcgcata actcgcgggg acagaggtga 180 acttagggta ttcgtcattg cttaa 205 40 24 DNA Artificial Sequence Description of Artificial Sequence primer 40 acgagaaggc gttgctgtag acca 24 41 24 DNA Artificial Sequence Description of Artificial Sequence primer 41 agcttgattt tcagcgaggg gatg 24 42 22 DNA Artificial Sequence Description of Artificial Sequence primer 42 acctcaacct ccacccattc tc 22 43 23 DNA Artificial Sequence Description of Artificial Sequence primer 43 cttctcgaac gtgatcttga tgc 23 44 25 DNA Artificial Sequence Description of Artificial Sequence primer 44 atgttgtcga agtcgcggct cacca 25 45 20 DNA Artificial Sequence Description of Artificial Sequence primer 45 tagctccttg gcagcctcat 20 46 23 DNA Artificial Sequence Description of Artificial Sequence primer 46 gtgacttcat caatacccga ctg 23 47 24 DNA Artificial Sequence Description of Artificial Sequence primer 47 gctcaaccat ggcttctcta cttc 24 48 24 DNA Artificial Sequence Description of Artificial Sequence primer 48 cacttttatt gagccacctg gtag 24 49 24 DNA Artificial Sequence Description of Artificial Sequence primer 49 ctgaccaaga gtgatgggaa gaag 24 50 24 DNA Artificial Sequence Description of Artificial Sequence primer 50 caagagtacg agatgagaat gcac 24 51 22 DNA Artificial Sequence Description of Artificial Sequence primer 51 acgagaaggc gctgctgtag ac 22 52 21 DNA Artificial Sequence Description of Artificial Sequence primer 52 gcgctcagca gcttgatttt c 21 53 22 DNA Artificial Sequence Description of Artificial Sequence primer 53 ttgctctcct cgatcgattg ac 22 54 22 DNA Artificial Sequence Description of Artificial Sequence primer 54 atcgccgtcg tggtcatctt gc 22 55 21 DNA Artificial Sequence Description of Artificial Sequence primer 55 ccgatgatct caaacttgtg a 21 56 27 DNA Artificial Sequence Description of Artificial Sequence primer 56 gtccttgctg acaacatcga tcctctg 27 57 26 DNA Artificial Sequence Description of Artificial Sequence primer 57 tcgccattga ttttctctgt ctgctc 26 58 25 DNA Artificial Sequence Description of Artificial Sequence primer 58 gaagcttgac tttgagcgca gccac 25 59 27 DNA Artificial Sequence Description of Artificial Sequence primer 59 gacgccgtgg ctgcgctcaa agtcaag 27 60 25 DNA Artificial Sequence Description of Artificial Sequence primer 60 gtggactacg cggcgggcac cggcg 25 61 23 DNA Artificial Sequence Description of Artificial Sequence primer 61 tcraayttrt gngcnarngt ngc 23 62 8 PRT Artificial Sequence Description of Artificial Sequence peptide 62 Ala Thr Leu Ala His Lys Phe Glu 1 5 63 17 DNA Artificial Sequence Description of Artificial Sequence primer 63 atnckytgra anacytg 17 64 6 PRT Artificial Sequence Description of Artificial Sequence peptide 64 Gln Val Phe Gln Arg Ile 1 5 65 23 DNA Artificial Sequence Description of Artificial Sequence primer 65 gtnwsnggny tnaaymgngg nyt 23 66 8 PRT Artificial Sequence Description of Artificial Sequence peptide 66 Val Ser Gly Leu Asn Arg Gly Leu 1 5 67 23 DNA Artificial Sequence Description of Artificial Sequence primer 67 ggncargtnt tycarmgnat hga 23 68 8 PRT Artificial Sequence Description of Artificial Sequence peptide 68 Gly Gln Val Phe Gln Arg Ile Asp 1 5 69 6 PRT Artificial Sequence Description of Artificial Sequence peptide 69 Gly Leu Asn Arg Gly Leu 1 5 70 6 PRT Artificial Sequence Description of Artificial Sequence peptide 70 Tyr Ser Ser Ala Phe Ser 1 5 71 10 PRT Artificial Sequence Description of Artificial Sequence peptide 71 Thr Leu Gly Gln Val Phe Gln Arg Ile Asp 1 5 10 72 5 PRT Artificial Sequence Description of Artificial Sequence peptide 72 Asp Phe Asp Asn Ile 1 5 73 9 PRT Artificial Sequence Description of Artificial Sequence peptide 73 Thr Ala Thr Leu Ala His Lys Phe Glu 1 5 74 5 PRT Artificial Sequence Description of Artificial Sequence peptide 74 Thr Arg Gly Asp Arg 1 5 75 6 PRT Artificial Sequence Description of Artificial Sequence peptide 75 Glu Leu Arg Val Phe Val 1 5 76 6 PRT Artificial Sequence Description of Artificial Sequence peptide 76 Ala Ala Xaa Xaa Leu Glu 1 5 77 14 PRT Artificial Sequence Description of Artificial Sequence peptide 77 Leu Gln Gly Xaa Trp Xaa Leu Xaa Tyr Ser Ser Ala Phe Ser 1 5 10 78 5 PRT Artificial Sequence Description of Artificial Sequence peptide 78 Arg Xaa Leu Gly Gly 1 5 79 17 PRT Artificial Sequence Description of Artificial Sequence peptide 79 Gly Arg Leu Xaa Pro Xaa Thr Leu Gly Gln Val Phe Gln Arg Ile Asp 1 5 10 15 Xaa 80 10 PRT Artificial Sequence Description of Artificial Sequence peptide 80 Thr Ala Thr Leu Ala His Lys Phe Glu Xaa 1 5 10 81 5 PRT Artificial Sequence Description of Artificial Sequence peptide 81 Thr Xaa Val Lys Thr 1 5 82 5 PRT Artificial Sequence Description of Artificial Sequence peptide 82 Val Thr Xaa Xaa Asp 1 5 83 7 PRT Artificial Sequence Description of Artificial Sequence peptide 83 Arg Xaa Thr Arg Gly Asp Arg 1 5 84 7 PRT Artificial Sequence Description of Artificial Sequence peptide 84 Glu Leu Arg Val Phe Val Xaa 1 5 85 92 PRT Artificial Sequence Description of Artificial Sequence primer 85 Xaa Gly Leu Asn Arg Gly Leu Xaa Tyr Ser Ser Ala Phe Ser Xaa Xaa 1 5 10 15 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 20 25 30 Xaa Thr Leu Gly Gln Val Phe Gln Arg Ile Asp Xaa Xaa Xaa Xaa Asp 35 40 45 Phe Asp Asn Ile Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 50 55 60 Xaa Xaa Xaa Xaa Thr Ala Thr Leu Ala His Lys Phe Glu Xaa Thr Arg 65 70 75 80 Gly Asp Arg Xaa Glu Leu Arg Val Phe Val Xaa Xaa 85 90 86 146 PRT Artificial Sequence Description of Artificial Sequence primer 86 Xaa Gly Leu Asn Arg Gly Leu Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 1 5 10 15 Xaa Xaa Xaa Ala Ala Xaa Xaa Leu Glu Xaa Leu Gln Gly Xaa Trp Xaa 20 25 30 Leu Xaa Tyr Ser Ser Ala Phe Ser Xaa Arg Xaa Leu Gly Gly Xaa Xaa 35 40 45 Xaa Xaa Xaa Xaa Xaa Gly Arg Leu Xaa Pro Xaa Thr Leu Gly Gln Val 50 55 60 Phe Gln Arg Ile Asp Xaa Xaa Xaa Xaa Asp Phe Asp Asn Ile Xaa Xaa 65 70 75 80 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Thr Ala 85 90 95 Thr Leu Ala His Lys Phe Glu Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 100 105 110 Xaa Xaa Xaa Xaa Thr Xaa Val Lys Thr Xaa Val Thr Xaa Xaa Asp Xaa 115 120 125 Xaa Xaa Arg Xaa Thr Arg Gly Asp Arg Xaa Glu Leu Arg Val Phe Val 130 135 140 Xaa Xaa 145 

What is claimed:
 1. An isolated protein which serves as a receptor in plants for plant pathogen hypersensitive response elicitors.
 2. A protein according to claim 1, wherein the plant pathogen is selected from the group consisting of Erwinia, Pseudomonas, Xanthamonas, Phytophthora, and Clavibacter.
 3. A protein according to claim 2, wherein the plant pathogen is an Erwinia pathogen.
 4. A protein according to claim 3, wherein the plant pathogen is Erwinia amylovora.
 5. A protein according to claim 1, wherein the protein is from a monocot.
 6. A protein according to claim 5, wherein the protein is from rice, barley, wheat, or maize.
 7. A protein according to claim 1, wherein the protein comprises an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or
 24. 8. A protein according to claim 1, wherein the protein is from a dicot.
 9. A protein according to claim 8, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape.
 10. A protein according to claim 1, wherein the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or
 34. 11. A protein according to claim 1, wherein the protein is recombinant.
 12. A protein according to claim 1, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof.
 13. A protein according to claim 1, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof.
 14. A protein according to claim 1, wherein the protein has an amino acid sequence of SEQ ID. No.
 85. 15. A protein according to claim 1, wherein the protein has an amino acid sequence of SEQ ID. No.
 86. 16. An isolated nucleic acid molecule encoding a protein according to claim
 1. 17. A nucleic acid molecule according to claim 16, wherein the plant pathogen is selected from the group consisting of Erwinia, Pseudomonas, Xanthamonas, Phytophthora, and Clavibacter.
 18. A nucleic acid molecule according to claim 17, wherein the plant pathogen is an Erwinia pathogen.
 19. A nucleic acid molecule according to claim 18, wherein the plant pathogen is Erwinia amylovora.
 20. A nucleic acid molecule according to claim 16, wherein the protein is from a monocot.
 21. A nucleic acid molecule according to claim 20, wherein the protein is from rice, barley, wheat, or maize.
 22. A nucleic acid molecule according to claim 16, wherein the protein comprises an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or
 24. 23. A nucleic acid molecule according to claim 16, wherein the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.
 24. A nucleic acid molecule according to claim 16, wherein the nucleic acid has a nucleotide sequence comprising SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or
 25. 25. A nucleic acid molecule according to claim 16, wherein the protein is from a dicot.
 26. A nucleic acid molecule according to claim 25, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape.
 27. A nucleic acid molecule according to claim 25, wherein the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or
 34. 28. A nucleic acid molecule according to claim 25, wherein the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.
 29. A nucleic acid molecule according to claim 25, wherein the nucleic acid has a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or
 35. 30. A nucleic acid according to claim 25, wherein the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC buffer at a temperature of 42° C.
 31. A nucleic acid according to claim 25, wherein the nucleic acid has a nucleotide sequence comprising SEQ. ID. No.
 3. 32. A nucleic acid according to claim 16, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof.
 33. A nucleic acid according to claim 16, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof.
 34. A nucleic acid according to claim 16, wherein the protein has an amino acid sequence of SEQ ID. No.
 85. 35. A nucleic acid according to claim 16, wherein the protein has an amino acid sequence of SEQ ID. No.
 86. 36. An antisense nucleic acid molecule to the nucleic acid according to claim
 16. 37. An expression vector containing a nucleic acid molecule according to claim 16 which is heterologous to the expression vector.
 38. An expression vector according to claim 37, wherein the nucleic acid molecule is positioned in the expression vector in sense orientation and correct reading frame.
 39. An expression vector according to claim 37, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 40. An expression vector containing a nucleic acid molecule according to claim 36 which is heterologous to the expression vector.
 41. A transgenic host cell transformed with the nucleic acid molecule according to claim
 16. 42. A host cell transformed according to claim 41, wherein the host cell is selected from the group consisting of a plant cell, a bacterial cell, and a fungal cell.
 43. A host cell according to claim 41, wherein the DNA molecule is transformed with an expression system.
 44. A host cell according to claim 41, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 45. A host cell transformed with a nucleic acid molecule according to claim
 36. 46. A transgenic plant transformed with the DNA molecule of claim
 16. 47. A transgenic plant according to claim 46, wherein the plant is selected from the group consisting of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane.
 48. A transgenic plant according to claim 46, wherein the plant is selected from the group consisting of Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.
 49. A transgenic plant according to claim 46, wherein the plant is a monocot.
 50. A transgenic plant according to claim 46, wherein the plant is from a dicot.
 51. A transgenic plant according to claim 46, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1,
 6. 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at atemperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the the motif of SEQ ID. No. 76, motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 52. A transgenic plant transformed with a nucleic acid molecule according to claim
 36. 53. A transgenic plant seed transformed with the DNA molecule of claim
 16. 54. A transgenic plant seed according to claim 53, wherein the plant is selected from the group consisting of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane.
 55. A transgenic plant seed according to claim 53, wherein the plant is selected from the group consisting of Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.
 56. A transgenic plant seed according to claim 53, wherein the plant is a monocot.
 57. A transgenic plant seed according to claim 53, wherein the plant is a dicot.
 58. A transgenic plant seed according to claim 53, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% fonmaride in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11,15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 59. A transgenic plant seed transformed with a nucleic acid molecule according to claim
 36. 60. A method of identifying agents targeting plant cells comprising: forming a reaction mixture comprising a protein according to claim 1 and a candidate agent; evaluating the reaction mixture for binding between the protein and the candidate agent; and identifying candidate compounds which bind to the protein in the reaction mixture as plant cell targeting agents.
 61. A method according to claim 60, wherein the protein is from a monocot.
 62. A method according to claim 60, wherein the protein is from rice, barley, wheat, or maize.
 63. A method according to claim 60, wherein the protein has an amino acid sequence comprises SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or
 24. 64. A method according to claim 60, wherein the protein is from a dicot.
 65. A method according to claim 64, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape.
 66. A method according to claim 60, wherein the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or
 34. 67. A method according to claim 60, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof.
 68. A method according to claim 60, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof.
 69. A method according to claim 60, wherein the protein has an amino acid sequence of SEQ ID. No.
 85. 70. A method according to claim 60, wherein the protein has an amino acid sequence of SEQ ID. No.
 86. 71. A method of identifying agents targeting plant cells comprising: forming a reaction mixture comprising a host cell transformed with a nucleic acid molecule according to claim 16 and a candidate agent; evaluating the reaction mixture for binding between protein produced by the host cell and the candidate agent; and identifying candidate compounds which bind to the protein produced by the host cell in the reaction mixture as plant cell targeting agents.
 72. A method according to claim 71, wherein the protein is from a monocot.
 73. A method according to claim 72, wherein the protein is from rice, barley, wheat, or maize.
 74. A method according to claim 71, wherein the protein is from a dicot.
 75. A method according to claim 71, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape.
 76. A method according to claim 71, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at atemperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; or (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or
 25. 77. A method according to claim 71, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof.
 78. A method according to claim 71, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof.
 79. A method according to claim 71, wherein the protein has an amino acid sequence of SEQ ID. No.
 85. 80. A method according to claim 71, wherein the protein has an amino acid sequence of SEQ ID. No.
 86. 81. A method of enhancing plant receptivity to treatment with hypersensitive response elicitors comprising: providing a transgenic plant or transgenic plant seed transformed with the nucleic acid molecule according to claim
 16. 82. A method according to claim 81, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; or (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or
 25. 83. A method according to claim 81, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof
 84. A method according to claim 81, wherein the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof.
 85. A method according to claim 81, wherein the protein has an amino acid sequence of SEQ ID. No.
 85. 86. A method according to claim 8 1, wherein the protein has an amino acid sequence of SEQ ID. No.
 86. 87. A method according to claim 8 1, wherein a transgenic plant is provided.
 88. A method according to claim 8 1, wherein a transgenic plant seed is provided and said method further comprises: planting the plant seeds under conditions effective for plants to grow from the planted plant seeds.
 89. A method according to claim 81, wherein the plant is selected from the group consisting of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, turnip, cauliflower, broccoli, radish, spinach, onion, garlic, eggplant, pepper, celery, parrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane.
 90. A method according to claim 81, wherein the plant is selected from the group consisting of Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.
 91. A method according to claim 81, wherein the hypersensitive response elicitor treatment is for imparting disease resistance.
 92. A method according to claim 81, wherein the hypersensitive response elicitor treatment is for enhancing plant growth.
 93. A method according to claim 81, wherein the hypersensitive response elicitor treatment is for controlling insects.
 94. A method according to claim 81, wherein the hypersensitive response elicitor treatment is for imparting stress tolerance.
 95. A method according to claim 81, wherein the transgenic plant or plant seed is further transformed with a second nucleic acid encoding a hypersensitive response elicitor, wherein expression of the second nucleic acid effects the hypersensitive response elicitor treatment.
 96. A method according to claim 81, wherein the hypersensitive response elicitor treatment comprises: applying a hypersensitive response elicitor to the plant or plant seed.
 97. A method according to claim 96, wherein the hypersensitive response elicitor is applied in isolated form.
 98. A method of imparting disease resistance, enhancing growth, controlling insects, and/or imparting stress resistance to plants comprising: providing a transgenic plant or transgenic plant seed transformed with a DNA construct effective to silence expression of a nucleic acid molecule according to claim
 16. 99. A method according to claim 98, wherein the protein is from a monocot.
 100. A method according to claim 99, wherein the protein is from rice, barley, wheat, or maize.
 101. A method according to claim 98, wherein the protein is from a dicot.
 102. A method according to claim 101, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape.
 103. A method according to claim 98, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 104. A method according to claim 98, wherein a transgenic plant is provided.
 105. A method according to claim 98, wherein a transgenic plant seed is provided and said method further comprises: planting the plant seeds under conditions effective for plants to grow from the planted plant seeds.
 106. A method according to claim 98, wherein the plant is selected from the group consisting of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, turnip, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane.
 107. A method according to claim 98, wherein the plant is selected from the group consisting of Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.
 108. A method according to claim 98, wherein the transgenic plant or plant seed is further transformed with a second nucleic acid encoding a hypersensitive response elicitor, wherein expression of the second nucleic acid effects a hypersensitive response elicitor treatment.
 109. A method according to claim 98 further comprising: applying a hypersensitive response elicitor to the plant or plant seed.
 110. A method according to claim 98, wherein the hypersensitive response elicitor is applied in isolated form.
 111. A method according to claim 98, wherein disease resistance is imparted to plants.
 112. A method according to claim 98, wherein enhanced growth is imparted to plants.
 113. A method according to claim 98, wherein insect control is imparted to plants.
 114. A method according to claim 98, wherein stress resistance is imparted to plants.
 115. A method according to claim 98, wherein the DNA construct is an antisense nucleic acid molecule to a nucleic acid molecule encoding a receptor in plants for plant pathogen hypersensitive response elicitors.
 116. A method according to claim 98, wherein the DNA construct is transcribable to a first nucleic acid encoding a receptor in plants for plant pathogen hypersensitive response elicitors coupled to a second nucleic acid encoding the inverted complement of the first nucleic acid.
 117. A method of imparting disease resistance, enhancing growth, controlling insects, and/or imparting stress resistance to plants comprising: providing a transgenic plant or transgenic plant seed transformed with the nucleic acid molecule according to claim
 16. 118. A method according to claim 117, wherein either: (1) the protein has an amino acid sequence of SEQ. ID. Nos. 1, 6, 8, 12, 18, 26, 28, 30, 32, or 34; (2) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, 35, or 39 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (3) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 2, 7, 9, 13, 19, 27, 29, 31, 33, or 35; (4) the nucleic acid hybridizes to a nucleotide sequence of SEQ. ID. No. 3 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9M saline/0.09M SSC at a temperature of 42° C.; (5) the nucleic acid comprises a nucleotide sequence of SEQ. ID. No. 3; (6) the protein has an amino acid sequence of SEQ. ID. Nos. 4, 10, 14, 16, 20, 22, or 24; (7) the nucleic acid hybridizes to the nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25 under stringent conditions of hybridization in buffer comprising 20% formamide in 0.9 M saline/0.09M SSC at a temperature of 42° C.; (8) the nucleic acid comprises a nucleotide sequence of SEQ. ID. Nos. 5, 11, 15, 17, 21, 23, or 25; (9) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 69, the motif of SEQ ID. No. 70, the motif of SEQ ID. No. 71, the motif of SEQ ID. No. 72, the motif of SEQ ID. No. 73, the motif of SEQ ID. No. 74, the motif of SEQ ID. No. 75, and combinations thereof; (10) the protein has an amino acid motif selected from the group consisting of the motif of SEQ ID. No. 76, the motif of SEQ ID. No. 77, the motif of SEQ ID. No. 78, the motif of SEQ ID. No. 79, the motif of SEQ ID. No. 80, the motif of SEQ ID. No. 81, the motif of SEQ ID. No. 82, the motif of SEQ ID. No. 83, the motif of SEQ ID. No. 84, and combinations thereof; (11) the protein has an amino acid sequence of SEQ ID. No. 85; or (12) the protein has an amino acid sequence of SEQ ID. No.
 86. 119. A method according to claim 117, wherein a transgenic plant is provided.
 120. A method according to claim 117, wherein a transgenic plant seed is provided and said method further comprises: planting the plant seeds under conditions effective for plants to grow from the planted plant seeds.
 121. A method according to claim 117, wherein the plant is selected from the group consisting of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, pea, chicory, lettuce, endive, cabbage, brussel sprout, beet, parsnip, turnip, cauliflower, broccoli, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugarcane.
 122. A method according to claim 117, wherein the plant is selected from the group consisting of Arabidopsis thaliana, Saintpaulia, petunia, pelargonium, poinsettia, chrysanthemum, carnation, and zinnia.
 123. A method according to claim 117, wherein disease resistance is imparted.
 124. A method according to claim 117, wherein plant growth is enhanced.
 125. A method according to claim 117, wherein insects are controlled.
 126. A method according to claim 117, wherein stress tolerance is imparted.
 127. A method according to claim 117, wherein the protein is from a monocot.
 128. A method according to claim 127, wherein the protein is from rice, barley, wheat, or maize.
 129. A method according to claim 117, wherein the protein is from a dicot.
 130. A method according to claim 129, wherein the protein is from Arabidopsis thaliana, cotton, soybean, tomato, potato, grapefruit, apple, tobacco, or grape. 